{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,21]],"date-time":"2026-02-21T22:24:55Z","timestamp":1771712695223,"version":"3.50.1"},"reference-count":77,"publisher":"Wiley","issue":"7","license":[{"start":{"date-parts":[[2014,2,19]],"date-time":"2014-02-19T00:00:00Z","timestamp":1392768000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2014,4]]},"abstract":"<jats:sec><jats:label\/><jats:p>Carbonic anhydrases (<jats:styled-content style=\"fixed-case\">CA<\/jats:styled-content>s) are metalloenzymes catalyzing the reversible hydration of carbon dioxide to bicarbonate (hydrogen carbonate) and protons. <jats:styled-content style=\"fixed-case\">CA<\/jats:styled-content>s have been identified in archaea, bacteria and eukaryotes and can be classified into five groups (\u03b1, \u03b2, \u03b3, \u03b4, \u03b6) that are unrelated in sequence and structure. The fungal \u03b2\u2010class has only recently attracted attention. In the present study, we investigated the structure and function of the plant\u2010like \u03b2\u2010<jats:styled-content style=\"fixed-case\">CA<\/jats:styled-content> proteins <jats:styled-content style=\"fixed-case\">CAS<\/jats:styled-content>1 and <jats:styled-content style=\"fixed-case\">CAS<\/jats:styled-content>2 from the filamentous ascomycete <jats:italic>Sordaria\u00a0macrospora<\/jats:italic>. We demonstrated that both proteins can substitute for the <jats:italic>Saccharomyces\u00a0cerevisiae<\/jats:italic> \u03b2\u2010<jats:styled-content style=\"fixed-case\">CA<\/jats:styled-content> Nce103 and exhibit an <jats:italic>in\u00a0vitro <\/jats:italic><jats:styled-content style=\"fixed-case\">CO<\/jats:styled-content><jats:sub>2<\/jats:sub> hydration activity (<jats:italic>k<\/jats:italic><jats:sub>cat<\/jats:sub>\/<jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub> of <jats:styled-content style=\"fixed-case\">CAS<\/jats:styled-content>1:\u00a01.30\u00a0\u00d7\u00a010<jats:sup>6<\/jats:sup>\u00a0<jats:sc>m<\/jats:sc><jats:sup>\u22121<\/jats:sup>\u00b7s<jats:sup>\u22121<\/jats:sup>; <jats:styled-content style=\"fixed-case\">CAS<\/jats:styled-content>2:\u00a01.21\u00a0\u00d7\u00a010<jats:sup>6\u00a0<\/jats:sup><jats:sc>m<\/jats:sc><jats:sup>\u22121<\/jats:sup>\u00b7s<jats:sup>\u22121<\/jats:sup>). To further investigate the structural properties of <jats:styled-content style=\"fixed-case\">CAS<\/jats:styled-content>1 and <jats:styled-content style=\"fixed-case\">CAS<\/jats:styled-content>2, we determined their crystal structures to a resolution of 2.7\u00a0\u00c5 and 1.8\u00a0\u00c5, respectively. The oligomeric state of both proteins is tetrameric. With the exception of the active site composition, no further major differences have been found. In both enzymes, the Zn<jats:sup>2<\/jats:sup><jats:sup>+<\/jats:sup>\u00a0\u2010ion is tetrahedrally coordinated; in <jats:styled-content style=\"fixed-case\">CAS<\/jats:styled-content>1 by Cys45, His101 and Cys104 and a water molecule and in <jats:styled-content style=\"fixed-case\">CAS<\/jats:styled-content>2 by the side chains of four residues (Cys56, His112, Cys115 and Asp58). Both <jats:styled-content style=\"fixed-case\">CA<\/jats:styled-content>s are only weakly inhibited by anions, making them good candidates for industrial applications.<\/jats:p><\/jats:sec><jats:sec><jats:title>Structured digital abstract<\/jats:title><jats:p><jats:list list-type=\"bullet\">\n<jats:list-item><jats:p><jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.uniprot.org\/uniprot\/C1L335\">CAS1<\/jats:ext-link>\u00a0and\u00a0<jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.uniprot.org\/uniprot\/C1L336\">CAS2<\/jats:ext-link>\u00a0<jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.ebi.ac.uk\/ontology-lookup\/?termId=MI:0407\">bind<\/jats:ext-link>\u00a0by\u00a0<jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.ebi.ac.uk\/ontology-lookup\/?termId=MI:0114\">x-ray crystallography<\/jats:ext-link>\u00a0(<jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.ebi.ac.uk\/intact\/interaction\/EBI-9107986\">View interaction<\/jats:ext-link>)<\/jats:p><\/jats:list-item>\n<\/jats:list><\/jats:p><\/jats:sec><jats:sec><jats:title>Database<\/jats:title><jats:p>Structural data have been deposited in the Protein Data Bank database under accession numbers <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.rcsb.org\/pdb\/search\/structidSearch.do?structureId=4O1J\">4O1J<\/jats:ext-link> for CAS1 and <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.rcsb.org\/pdb\/search\/structidSearch.do?structureId=4O1K\">4O1K<\/jats:ext-link> for CAS2.<\/jats:p><\/jats:sec>","DOI":"10.1111\/febs.12738","type":"journal-article","created":{"date-parts":[[2014,2,7]],"date-time":"2014-02-07T14:43:07Z","timestamp":1391784187000},"page":"1759-1772","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":43,"title":["Crystal structures of two tetrameric \u03b2\u2010carbonic anhydrases from the filamentous ascomycete <i>Sordaria\u00a0macrospora<\/i>"],"prefix":"10.1111","volume":"281","author":[{"given":"Ronny","family":"Lehneck","sequence":"first","affiliation":[{"name":"Institute of Microbiology and Genetics Department of Genetics of Eukaryotic Microorganisms Georg\u2010August\u2010University G\u00f6ttingen Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Piotr","family":"Neumann","sequence":"additional","affiliation":[{"name":"Institute of Microbiology and Genetics Department of Molecular Structural Biology Georg\u2010August\u2010University G\u00f6ttingen 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