4G7A
The crystal structure of an alpha Carbonic Anhydrase from the extremophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1
Summary for 4G7A
| Entry DOI | 10.2210/pdb4g7a/pdb |
| Related | 1CA2 1KOP |
| Descriptor | Carbonate dehydratase, ZINC ION, 5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE, ... (4 entities in total) |
| Functional Keywords | lyase |
| Biological source | Sulfurihydrogenibium sp. YO3AOP1 (Sulfurihydrogenibium yellowstonense) |
| Total number of polymer chains | 2 |
| Total formula weight | 58083.43 |
| Authors | Di Fiore, A.,De Simone, G. (deposition date: 2012-07-20, release date: 2013-05-29, Last modification date: 2024-11-27) |
| Primary citation | Di Fiore, A.,Capasso, C.,De Luca, V.,Monti, S.M.,Carginale, V.,Supuran, C.T.,Scozzafava, A.,Pedone, C.,Rossi, M.,De Simone, G. X-ray structure of the first `extremo-{alpha}-carbonic anhydrase', a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1. Acta Crystallogr.,Sect.D, 69:1150-1159, 2013 Cited by PubMed Abstract: SspCA, a novel `extremo-α-carbonic anhydrase' isolated from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1, is an efficient catalyst for the hydration of CO2 and presents exceptional thermostability. Indeed, SspCA retains a high catalytic activity even after being heated to 343-373 K for several hours. Here, the crystallographic structure of this α-carbonic anhydrase (α-CA) is reported and the factors responsible for its function at high temperature are elucidated. In particular, the study suggests that increased structural compactness, together with an increased number of charged residues on the protein surface and a greater number of ionic networks, seem to be the key factors involved in the higher thermostability of this enzyme with respect to its mesophilic homologues. These findings are of extreme importance, since they provide a structural basis for the understanding of the mechanisms responsible for thermal stability in the α-CA family for the first time. The data obtained offer a tool that can be exploited to engineer α-CAs in order to obtain enzymes with enhanced thermostability for use in the harsh conditions of the CO2 capture and sequestration processes. PubMed: 23695259DOI: 10.1107/S0907444913007208 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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