{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,25]],"date-time":"2026-03-25T14:21:24Z","timestamp":1774448484351,"version":"3.50.1"},"reference-count":45,"publisher":"Elsevier BV","issue":"7","license":[{"start":{"date-parts":[[1995,7,1]],"date-time":"1995-07-01T00:00:00Z","timestamp":804556800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2013,7,17]],"date-time":"2013-07-17T00:00:00Z","timestamp":1374019200000},"content-version":"vor","delay-in-days":6591,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Structure"],"published-print":{"date-parts":[[1995,7]]},"DOI":"10.1016\/s0969-2126(01)00207-6","type":"journal-article","created":{"date-parts":[[2004,7,23]],"date-time":"2004-07-23T19:10:35Z","timestamp":1090609835000},"page":"729-741","source":"Crossref","is-referenced-by-count":124,"title":["Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition"],"prefix":"10.1016","volume":"3","author":[{"given":"Andrea","family":"Mattevi","sequence":"first","affiliation":[]},{"given":"Giovanna","family":"Valentini","sequence":"additional","affiliation":[]},{"given":"Menico","family":"Rizzi","sequence":"additional","affiliation":[]},{"given":"M.Luisa","family":"Speranza","sequence":"additional","affiliation":[]},{"given":"Martino","family":"Bolognesi","sequence":"additional","affiliation":[]},{"given":"Alessandro","family":"Coda","sequence":"additional","affiliation":[]}],"member":"78","reference":[{"key":"10.1016\/S0969-2126(01)00207-6_BIB1","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1016\/S0021-9258(18)44993-9","article-title":"The role of potassium in muscle phosphorylation","volume":"146","author":"Boyer","year":"1942","journal-title":"J. Biol. Chem"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB2","doi-asserted-by":"crossref","first-page":"2881","DOI":"10.1021\/bi00658a028","article-title":"Dual divalent cation requirement for activation of pyruvate kinase: essential roles of both enzyme-\u00a0 and nucleotide-bound metal ion","volume":"15","author":"Gupta","year":"1976","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB3","series-title":"The Enzymes,","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1016\/S1874-6047(08)60071-2","article-title":"Pyruvate kinase","author":"Kayne","year":"1973"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB4","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/0079-6107(93)90001-Z","article-title":"Evolution of glycolysis","volume":"59","author":"Fothergill","year":"1992","journal-title":"Progr. Mol. Biol. Biophys"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB5","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1042\/bj1890421","article-title":"Analysis of progress curves: rate law of pyruvate kinase type I from E. coli.","volume":"189","author":"Markus","year":"1980","journal-title":"J. Biochem"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB6","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1002\/j.1460-2075.1986.tb04236.x","article-title":"Structure of cat muscle pyruvate kinase","volume":"5","author":"Muirhead","year":"1986","journal-title":"EMBO J"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB7","doi-asserted-by":"crossref","first-page":"6301","DOI":"10.1021\/bi00186a033","article-title":"Structure of rabbit muscle pyruvate kinase with Mn2+, K+, and pyruvate","volume":"33","author":"Larsen","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB8","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/0022-2836(92)90505-E","article-title":"Key residues in the allosteric transition of Bacillus stearothermophilus pyruvate kinase identified by site-directed mutagenesis","volume":"228","author":"Walker","year":"1992","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB9","doi-asserted-by":"crossref","first-page":"13807","DOI":"10.1016\/S0021-9258(18)67091-7","article-title":"The M1-\u00a0 and M2-type isozymes of rat pyruvate kinase are produced from the same gene by alternative RNA splicing","volume":"261","author":"Noguchi","year":"1986","journal-title":"J. Biol. Chem"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB10","doi-asserted-by":"crossref","first-page":"8756","DOI":"10.1021\/bi00448a012","article-title":"Effects of primary sequence differences on the global structure and function of an enzyme: a study of pyruvate kinase isozymes","volume":"28","author":"Consler","year":"1989","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB11","doi-asserted-by":"crossref","first-page":"1219","DOI":"10.1515\/bchm3.1988.369.2.1219","article-title":"Reactivity of the fructose-1,6-bisphosphate-activated pyruvate kinase from E. coli with pyridoxal 5\u2032-phosphate","volume":"369","author":"Valentini","year":"1988","journal-title":"Biol. Chem. Hoppe-Seyler"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB12","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1515\/bchm3.1989.370.1.211","article-title":"Primary structure of three peptides at the catalytic and allosteric sites of the fructose-1,6-bisphosphate-activated pyruvate kinase from E. coli.","volume":"370","author":"Speranza","year":"1989","journal-title":"Biol. Chem. Hoppe-Seyler"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB13","doi-asserted-by":"crossref","first-page":"6883","DOI":"10.1073\/pnas.86.18.6883","article-title":"Direct genomic sequencing of bacterial DNA: the pyruvate kinase I gene of Escherichia coli.","volume":"86","author":"Ohara","year":"1989","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB14","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/S0022-2836(65)80285-6","article-title":"On the nature of the allosteric transitions: a plausible model","volume":"12","author":"Monod","year":"1965","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB15","doi-asserted-by":"crossref","first-page":"3811","DOI":"10.1002\/j.1460-2075.1992.tb05472.x","article-title":"The cooperative binding of fructose-1,6-bisphosphate to yeast pyruvate kinase","volume":"11","author":"Murcott","year":"1992","journal-title":"EMBO J"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB16","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1002\/prot.340110307","article-title":"Analysis of the steric strain in the polypeptide backbone of protein molecules","volume":"11","author":"Herzberg","year":"1991","journal-title":"Proteins"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB17","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1016\/0959-440X(94)90272-0","article-title":"Domain movements in protein kinases","volume":"4","author":"Cox","year":"1994","journal-title":"Curr. Opin. Struct. Biol"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB18","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1038\/273443a0","article-title":"The \u03b1-helix dipole and the properties of proteins","volume":"273","author":"Hol","year":"1978","journal-title":"Nature"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB19","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1038\/340609a0","article-title":"The allosteric transition of glycogen phosphorylase","volume":"340","author":"Barford","year":"1989","journal-title":"Nature"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB20","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1038\/nsb0394-176","article-title":"T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control","volume":"1","author":"Iwata","year":"1994","journal-title":"Nat. Struct. Biol"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB21","doi-asserted-by":"crossref","first-page":"14111","DOI":"10.1021\/bi00214a006","article-title":"Stereochemistry of metal ion coordination to the terminal thiophosphoryl group of adenosine 5\u2032-O-(3-thiotriphosphate) at the active site of pyruvate kinase","volume":"32","author":"Buchbinder","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB22","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1002\/prot.340100105","article-title":"The crystal structure of the \u2018open\u2019 and the \u2018closed\u2019 conformation of the flexible loop of trypanosomal triosephosphate isomerase","volume":"10","author":"Wierenga","year":"1991","journal-title":"Proteins"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB23","doi-asserted-by":"crossref","first-page":"9968","DOI":"10.1073\/pnas.90.21.9968","article-title":"Formation of the active site of ribulose-1,5-bisphosphate carboxylase\/oxygenase by a disorder\u2013order transition from the unactivated to the activated form","volume":"90","author":"Schreuder","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB24","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1038\/343140a0","article-title":"Structural basis of the allosteric behaviour of phosphofructokinase","volume":"343","author":"Schirmer","year":"1990","journal-title":"Nature"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB25","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1006\/jmbi.1994.1755","article-title":"Toward a mechanism for the allosteric transition of pig kidney fructose-1,6-bisphosphatase","volume":"244","author":"Zhang","year":"1994","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB26","first-page":"in press","article-title":"Crystallization and preliminary X-ray analysis of pyruvate kinase type-I from Escherichia coli.","author":"Mattevi","year":"1995","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB27","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1107\/S0907444994003112","article-title":"The CCP4 suite: programs for protein crystallography","volume":"50","author":"Collaborative Computational Project Number 4","year":"1994","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB28","series-title":"Isomorphous Replacement and Anomalous Scattering: Proceedings of the CCP4 Study Weekend 25\u201326 January 1991","first-page":"23","article-title":"Heavy atom location using SHELXS-90","author":"Sheldrick","year":"1991"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB29","series-title":"Isomorphous Replacement and Anomalous Scattering: Proceedings of the CCP4 Study Weekend 25\u201326 January 1991","first-page":"80","article-title":"Maximum likelihood refinement of heavy atom parameters","author":"Otwinowski","year":"1991"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB30","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1016\/0022-2836(68)90205-2","article-title":"Solvent content of protein crystals","volume":"33","author":"Matthews","year":"1968","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB31","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1107\/S0108767390005530","article-title":"The locked rotation function","volume":"46","author":"Tong","year":"1990","journal-title":"Acta Crystallogr. A"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB32","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1107\/S0365110X62000067","article-title":"The detection of sub-units within the crystallographic asymmetric unit","volume":"15","author":"Rossmann","year":"1962","journal-title":"Acta Crystallogr"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB33","series-title":"Crystallographic Computing 5: From Chemistry to Biology","first-page":"361","article-title":"Density modification: theory and practice","author":"Podjarny","year":"1991"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB34","first-page":"in press","article-title":"DEMON: a program package for density modification and phase improvement","author":"Vellieux","year":"1995","journal-title":"J. Appl. Crystallogr"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB35","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1107\/S0108767390010224","article-title":"Improved methods for building models in electron density maps and the location of errors in these models","volume":"47","author":"Jones","year":"1991","journal-title":"Acta Crystallogr. A"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB36","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1126\/science.235.4787.458","article-title":"Crystallographic R-factor refinement by molecular dynamics","volume":"235","author":"Br\u00fcnger","year":"1987","journal-title":"Science"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB37","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1107\/S0108767386099622","article-title":"Improved Fourier coefficients for maps using phases from partial structures with errors","volume":"42","author":"Read","year":"1986","journal-title":"Acta Crystallogr. A"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB38","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1016\/S0969-2126(94)00116-2","article-title":"Cryocrystallography","volume":"2","author":"Rodgers","year":"1994","journal-title":"Structure"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB39","series-title":"Data collection and Processing","first-page":"56","article-title":"DENZO","author":"Otwinowski","year":"1993"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB40","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1107\/S0108767393007597","article-title":"AMORE: an automated procedure for molecular replacement","volume":"50","author":"Navaza","year":"1994","journal-title":"Acta Crystallogr. A"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB41","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1107\/S0567739480000794","article-title":"A restrained-parameter thermal-factor refinement procedure","volume":"36","author":"Konnert","year":"1980","journal-title":"Acta Crystallogr. A"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB42","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1107\/S0108767391001071","article-title":"Accurate bond angle and parameters for X-ray protein structure refinement","volume":"45","author":"Engh","year":"1991","journal-title":"Acta Crystallogr. A"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB43","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1038\/355472a0","article-title":"The free R value: a novel statistical quantity for assessing the accuracy of crystal structures","volume":"355","author":"Br\u00fcnger","year":"1992","journal-title":"Nature"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB44","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1107\/S0021889892009944","article-title":"PROCHECK: a program to check the stereochemistry of protein structures","volume":"26","author":"Laskowski","year":"1993","journal-title":"J. Appl. Crystallogr"},{"key":"10.1016\/S0969-2126(01)00207-6_BIB45","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1107\/S0021889891004399","article-title":"MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures","volume":"24","author":"Kraulis","year":"1991","journal-title":"J. Appl. Crystallogr"}],"container-title":["Structure"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212601002076?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212601002076?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,6,24]],"date-time":"2021-06-24T14:39:58Z","timestamp":1624545598000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0969212601002076"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1995,7]]},"references-count":45,"journal-issue":{"issue":"7","published-print":{"date-parts":[[1995,7]]}},"alternative-id":["S0969212601002076"],"URL":"https:\/\/doi.org\/10.1016\/s0969-2126(01)00207-6","relation":{},"ISSN":["0969-2126"],"issn-type":[{"value":"0969-2126","type":"print"}],"subject":[],"published":{"date-parts":[[1995,7]]}}}