| http://purl.uniprot.org/citations/11316870 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11316870 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11316870 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/11316870 | http://www.w3.org/2000/01/rdf-schema#comment | "Carbonic anhydrases fall into three distinct evolutionary and structural classes: alpha, beta, and gamma. The beta-class carbonic anhydrases (beta-CAs) are widely distributed among higher plants, simple eukaryotes, eubacteria, and archaea. We have determined the crystal structure of ECCA, a beta-CA from Escherichia coli, to a resolution of 2.0 A. In agreement with the structure of the beta-CA from the chloroplast of the red alga Porphyridium purpureum, the active-site zinc in ECCA is tetrahedrally coordinated by the side chains of four conserved residues. These results confirm the observation of a unique pattern of zinc ligation in at least some beta-CAS: The absence of a water molecule in the inner coordination sphere is inconsistent with known mechanisms of CA activity. ECCA activity is highly pH-dependent in the physiological range, and its expression in yeast complements an oxygen-sensitive phenotype displayed by a beta-CA-deletion strain. The structural and biochemical characterizations of ECCA presented here and the comparisons with other beta-CA structures suggest that ECCA can adopt two distinct conformations displaying widely divergent catalytic rates."xsd:string |
| http://purl.uniprot.org/citations/11316870 | http://purl.org/dc/terms/identifier | "doi:10.1110/ps.46301"xsd:string |
| http://purl.uniprot.org/citations/11316870 | http://purl.org/dc/terms/identifier | "doi:10.1110/ps.46301"xsd:string |
| http://purl.uniprot.org/citations/11316870 | http://purl.org/dc/terms/identifier | "doi:10.1110/ps.46301"xsd:string |
| http://purl.uniprot.org/citations/11316870 | http://purl.uniprot.org/core/author | "Endrizzi J.A."xsd:string |
| http://purl.uniprot.org/citations/11316870 | http://purl.uniprot.org/core/author | "Endrizzi J.A."xsd:string |
| http://purl.uniprot.org/citations/11316870 | http://purl.uniprot.org/core/author | "Cronk J.D."xsd:string |
| http://purl.uniprot.org/citations/11316870 | http://purl.uniprot.org/core/author | "Cronk J.D."xsd:string |
| http://purl.uniprot.org/citations/11316870 | http://purl.uniprot.org/core/author | "Cronk M.R."xsd:string |
| http://purl.uniprot.org/citations/11316870 | http://purl.uniprot.org/core/author | "Cronk M.R."xsd:string |
| http://purl.uniprot.org/citations/11316870 | http://purl.uniprot.org/core/author | "O'neill J.W."xsd:string |
| http://purl.uniprot.org/citations/11316870 | http://purl.uniprot.org/core/author | "O'neill J.W."xsd:string |
| http://purl.uniprot.org/citations/11316870 | http://purl.uniprot.org/core/author | "Zhang K.Y.J."xsd:string |
| http://purl.uniprot.org/citations/11316870 | http://purl.uniprot.org/core/author | "Zhang K.Y.J."xsd:string |
| http://purl.uniprot.org/citations/11316870 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11316870 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11316870 | http://purl.uniprot.org/core/name | "Protein Sci."xsd:string |
| http://purl.uniprot.org/citations/11316870 | http://purl.uniprot.org/core/name | "Protein Sci."xsd:string |
| http://purl.uniprot.org/citations/11316870 | http://purl.uniprot.org/core/pages | "911-922"xsd:string |
| http://purl.uniprot.org/citations/11316870 | http://purl.uniprot.org/core/pages | "911-922"xsd:string |
| http://purl.uniprot.org/citations/11316870 | http://purl.uniprot.org/core/title | "Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity."xsd:string |
| http://purl.uniprot.org/citations/11316870 | http://purl.uniprot.org/core/title | "Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity."xsd:string |