4XZ5
Structure of the thermostable alpha-Carbonic Anydrase from Thiomicrospira crunogena XCL-2 gammaproteobacterium
Summary for 4XZ5
| Entry DOI | 10.2210/pdb4xz5/pdb |
| Descriptor | Carbonic anhydrase, alpha family, ZINC ION, BICARBONATE ION, ... (4 entities in total) |
| Functional Keywords | carbonic anhydrase, thiomicrospira crunogena xcl-2, thermostability, co2 sequestration, lyase |
| Biological source | Thiomicrospira crunogena (strain XCL-2) |
| Total number of polymer chains | 4 |
| Total formula weight | 107242.62 |
| Authors | Mahon, B.P.,Diaz-Torres, N.A.,Pinard, M.A.,McKenna, R. (deposition date: 2015-02-03, release date: 2015-07-29, Last modification date: 2024-11-13) |
| Primary citation | Diaz-Torres, N.A.,Mahon, B.P.,Boone, C.D.,Pinard, M.A.,Tu, C.,Ng, R.,Agbandje-McKenna, M.,Silverman, D.,Scott, K.,McKenna, R. Structural and biophysical characterization of the alpha-carbonic anhydrase from the gammaproteobacterium Thiomicrospira crunogena XCL-2: insights into engineering thermostable enzymes for CO2 sequestration. Acta Crystallogr.,Sect.D, 71:1745-1756, 2015 Cited by PubMed Abstract: Biocatalytic CO2 sequestration to reduce greenhouse-gas emissions from industrial processes is an active area of research. Carbonic anhydrases (CAs) are attractive enzymes for this process. However, the most active CAs display limited thermal and pH stability, making them less than ideal. As a result, there is an ongoing effort to engineer and/or find a thermostable CA to fulfill these needs. Here, the kinetic and thermal characterization is presented of an α-CA recently discovered in the mesophilic hydrothermal vent-isolate extremophile Thiomicrospira crunogena XCL-2 (TcruCA), which has a significantly higher thermostability compared with human CA II (melting temperature of 71.9°C versus 59.5°C, respectively) but with a tenfold decrease in the catalytic efficiency. The X-ray crystallographic structure of the dimeric TcruCA shows that it has a highly conserved yet compact structure compared with other α-CAs. In addition, TcruCA contains an intramolecular disulfide bond that stabilizes the enzyme. These features are thought to contribute significantly to the thermostability and pH stability of the enzyme and may be exploited to engineer α-CAs for applications in industrial CO2 sequestration. PubMed: 26249355DOI: 10.1107/S1399004715012183 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.596 Å) |
Structure validation
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