{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T21:35:49Z","timestamp":1779399349087,"version":"3.53.1"},"reference-count":67,"publisher":"Wiley","issue":"7","license":[{"start":{"date-parts":[[2008,12,31]],"date-time":"2008-12-31T00:00:00Z","timestamp":1230681600000},"content-version":"vor","delay-in-days":5297,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[1994,7]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The 3\u2010dimensional structure of inorganic pyrophosphatase from <jats:italic>Thermus thermophilus<\/jats:italic> (T\u2010PPase) has been determined by X\u2010ray diffraction at 2.0 \u00c5 resolution and refined to <jats:italic>R<\/jats:italic> = 15.3%. The structure consists of an antiparallel closed \u03b2\u2010sheet and 2 \u03b1\u2010helices and resembles that of the yeast enzyme in spite of the large difference in size (174 and 286 residues, respectively), little sequence similarity beyond the active center (about 20%), and different oligomeric organization (hexameric and dimeric, respectively). The similarity of the polypeptide folding in the 2 PPases provides a very strong argument in favor of an evolutionary relationship between the yeast and bacterial enzymes. The same Greek\u2010key topology of the 5\u2010stranded \u03b2\u2010barrel was found in the OB\u2010fold proteins, the bacteriophage gene\u20105 DNA\u2010binding protein, toxic\u2010shock syndrome toxin\u20101, and the major cold\u2010shock protein of <jats:italic>Bacillus subtilis.<\/jats:italic> Moreover, all known nucleotide\u2010binding sites in these proteins are located on the same side of the \u03b2\u2010barrel as the active center in T\u2010PPase. Analysis of the active center of T\u2010PPase revealed 17 residues of potential functional importance, 16 of which are strictly conserved in all sequences of soluble PPases. Their possible role in the catalytic mechanism is discussed on the basis of the present crystal structure and with respect to site\u2010directed mutagenesis studies on the <jats:italic>Escherichia coli<\/jats:italic> enzyme. The observed oligomeric organization of T\u2010PPase allows us to suggest a possible mechanism for the allosteric regulation of hexameric PPases.<\/jats:p>","DOI":"10.1002\/pro.5560030713","type":"journal-article","created":{"date-parts":[[2009,2,10]],"date-time":"2009-02-10T01:41:33Z","timestamp":1234230093000},"page":"1098-1107","source":"Crossref","is-referenced-by-count":54,"title":["Crystal structure of inorganic pyrophosphatase from <i>Thermus thermophilus<\/i>"],"prefix":"10.1002","volume":"3","author":[{"given":"Alexei","family":"Teplyakov","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Galya","family":"Obmolova","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Keith S.","family":"Wilson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Keisuke","family":"Ishii","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiroyuki","family":"Kaji","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tatsuya","family":"Samejima","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Inna","family":"Kuranova","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2008,12,31]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1038\/367094a0"},{"key":"e_1_2_1_3_1","first-page":"1113","article-title":"Interaction of inorganic pyrophosphatase with diisopropylfluorophosphate","volume":"35","author":"Avaeva SM","year":"1970","journal-title":"Biokhimiyu"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1990.tb19482.x"},{"key":"e_1_2_1_5_1","first-page":"796","article-title":"The interaction of phosphate and manganese ions with baker's yeast inorganic pyrophosphatase","volume":"54","author":"Baykov AA","year":"1989","journal-title":"Biokhimiya"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(77)80200-3"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00542a015"},{"key":"e_1_2_1_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(85)80654-2"},{"key":"e_1_2_1_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(83)80065-5"},{"key":"e_1_2_1_10_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.235.4787.458"},{"key":"e_1_2_1_11_1","doi-asserted-by":"crossref","first-page":"4346","DOI":"10.1016\/S0021-9258(19)63801-9","article-title":"Constitutive inorganic pyrophosphatase of Escherichia coli. 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