{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,18]],"date-time":"2026-07-18T10:49:06Z","timestamp":1784371746913,"version":"3.55.0"},"reference-count":36,"publisher":"National Academy of Sciences","issue":"6","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2010,2,9]]},"abstract":"<jats:p>\n                    Cyanobacterial RuBisCO is sequestered in large, icosahedral, protein-bounded microcompartments called carboxysomes. Bicarbonate is pumped into the cytosol, diffuses into the carboxysome through small pores in its shell, and is then converted to CO\n                    <jats:sub>2<\/jats:sub>\n                    by carbonic anhydrase (CA) prior to fixation. Paradoxically, many \u03b2-cyanobacteria, including\n                    <jats:italic>Thermosynechococcus elongatus<\/jats:italic>\n                    BP-1, lack the conventional carboxysomal \u03b2-CA,\n                    <jats:italic>ccaA<\/jats:italic>\n                    . The N-terminal domain of the carboxysomal protein CcmM is homologous to \u03b3-CA from\n                    <jats:italic>Methanosarcina thermophila<\/jats:italic>\n                    (Cam) but recombinant CcmM derived from\n                    <jats:italic>ccaA<\/jats:italic>\n                    -containing cyanobacteria show no CA activity. We demonstrate here that either full length CcmM from\n                    <jats:italic>T. elongatus<\/jats:italic>\n                    , or a construct truncated after 209 residues (CcmM209), is active as a CA\u2014the first catalytically active bacterial \u03b3-CA reported. The 2.0\u00a0\u212b structure of CcmM209 reveals a trimeric, left-handed \u03b2-helix structure that closely resembles Cam, except that residues 198\u2013207 form a third \u03b1-helix stabilized by an essential Cys194-Cys200 disulfide bond. Deleting residues 194\u2013209 (CcmM193) results in an inactive protein whose 1.1\u00a0\u212b structure shows disordering of the N- and C-termini, and reorganization of the trimeric interface and active site. Under reducing conditions, CcmM209 is similarly partially disordered and inactive as a CA. CcmM protein in fresh\n                    <jats:italic>E. coli<\/jats:italic>\n                    cell extracts is inactive, implying that the cellular reducing machinery can reduce and inactivate CcmM, while diamide, a thiol oxidizing agent, activates the enzyme. Thus, like membrane-bound eukaryotic cellular compartments, the \u03b2-carboxysome appears to be able to maintain an oxidizing interior by precluding the entry of thioredoxin and other endogenous reducing agents.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0910866107","type":"journal-article","created":{"date-parts":[[2010,1,25]],"date-time":"2010-01-25T21:54:47Z","timestamp":1264456487000},"page":"2455-2460","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":184,"title":["Structural basis of the oxidative activation of the carboxysomal \u03b3-carbonic anhydrase, CcmM"],"prefix":"10.1073","volume":"107","author":[{"given":"Kerry L.","family":"Pe\u00f1a","sequence":"first","affiliation":[{"name":"Department of Molecular and Cellular Biology, University of Guelph, Guelph, ON, Canada, N1G2W1"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephane E.","family":"Castel","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cellular Biology, University of Guelph, Guelph, ON, Canada, N1G2W1"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Charlotte","family":"de Araujo","sequence":"additional","affiliation":[{"name":"Departments of Cell and Systems Biology, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"George S.","family":"Espie","sequence":"additional","affiliation":[{"name":"Departments of Cell and Systems Biology, and"},{"name":"Biology, University of Toronto, Mississauga, ON, Canada L5L1C6"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthew S.","family":"Kimber","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cellular Biology, University of Guelph, Guelph, ON, Canada, N1G2W1"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2010,1,25]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.plaphy.2008.01.001"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1093\/jxb\/erg076"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0711165105"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2007.06.059"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2006.09.024"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pbio.0050144"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M709285200"},{"key":"e_1_3_3_8_2","first-page":"973","article-title":"The functioning of the CO2 concentrating mechanism in several cyanobacterial strains: A review of general physiological characteristics, genes, proteins, and recent advances","volume":"76","author":"Price GD","year":"1998","unstructured":"GD Price, et al., The functioning of the CO2 concentrating mechanism in several cyanobacterial strains: A review of general physiological characteristics, genes, proteins, and recent advances. Can J Bot 76, 973\u20131002 (1998).","journal-title":"Can J Bot"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1529-8817.2000.00028.x"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1139\/b91-124"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.01283-07"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.175.10.2871-2879.1993"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1139\/b05-058"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M703896200"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.89.10.4437"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1007\/s004250100638"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.91.15.6909"},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.1002\/j.1460-2075.1996.tb00588.x"},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1139\/b05-057"},{"key":"e_1_3_3_20_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bmcl.2004.09.085"},{"key":"e_1_3_3_21_2","doi-asserted-by":"publisher","DOI":"10.1007\/s11103-004-0149-7"},{"key":"e_1_3_3_22_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.185.21.6415-6424.2003"},{"key":"e_1_3_3_23_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00253-003-1402-8"},{"key":"e_1_3_3_24_2","doi-asserted-by":"publisher","DOI":"10.1104\/pp.103.037283"},{"key":"e_1_3_3_25_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi0001877"},{"key":"e_1_3_3_26_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi026831u"},{"key":"e_1_3_3_27_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1113397"},{"key":"e_1_3_3_28_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biochem.68.1.33"},{"key":"e_1_3_3_29_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi010768b"},{"key":"e_1_3_3_30_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi052507y"},{"key":"e_1_3_3_31_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja803928m"},{"key":"e_1_3_3_32_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1742-4658.2006.05421.x"},{"key":"e_1_3_3_33_2","doi-asserted-by":"publisher","DOI":"10.1104\/pp.91.2.505"},{"key":"e_1_3_3_34_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.micro.54.1.439"},{"key":"e_1_3_3_35_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2009.03.056"},{"key":"e_1_3_3_36_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1151458"}],"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.0910866107","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,14]],"date-time":"2022-04-14T05:10:57Z","timestamp":1649913057000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.0910866107"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2010,1,25]]},"references-count":36,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2010,2,9]]}},"alternative-id":["10.1073\/pnas.0910866107"],"URL":"https:\/\/doi.org\/10.1073\/pnas.0910866107","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[2010,1,25]]},"assertion":[{"value":"2010-01-25","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}