6YL7
Crystal structure of beta carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomallei
Summary for 6YL7
| Entry DOI | 10.2210/pdb6yl7/pdb |
| Descriptor | Beta carbonic anhydrase, ZINC ION (3 entities in total) |
| Functional Keywords | carbonic anhydrase, beta carbonic anhydrase, burkholderia pseudomallei, lyase |
| Biological source | Burkholderia pseudomallei |
| Total number of polymer chains | 1 |
| Total formula weight | 28334.42 |
| Authors | Angeli, A.,Ferraroni, M. (deposition date: 2020-04-06, release date: 2020-06-10, Last modification date: 2024-01-24) |
| Primary citation | Angeli, A.,Ferraroni, M.,Pinteala, M.,Maier, S.S.,Simionescu, B.C.,Carta, F.,Del Prete, S.,Capasso, C.,Supuran, C.T. Crystal Structure of a Tetrameric Type II beta-Carbonic Anhydrase from the Pathogenic BacteriumBurkholderia pseudomallei. Molecules, 25:-, 2020 Cited by PubMed Abstract: Carbonic anhydrase (CA) is a zinc enzyme that catalyzes the reversible conversion of carbon dioxide to bicarbonate and proton. Currently, CA inhibitors are widely used as antiglaucoma, anticancer, and anti-obesity drugs and for the treatment of neurological disorders. Recently, the potential use of CA inhibitors to fight infections caused by protozoa, fungi, and bacteria has emerged as a new research line. In this article, the X-ray crystal structure of β-CA from was reported. The X-ray crystal structure of this new enzyme was solved at 2.7 Å resolution, revealing a tetrameric type II β-CA with a "closed" active site in which the zinc is tetrahedrally coordinated to Cys46, Asp48, His102, and Cys105. is known to encode at least two CAs, a β-CA, and a γ-CA. These proteins, playing a pivotal role in its life cycle and pathogenicity, offer a novel therapeutic opportunity to obtain antibiotics with a different mechanism of action. Furthermore, the new structure can provide a clear view of the β-CA mechanism of action and the possibility to find selective inhibitors for this class of CAs. PubMed: 32408533DOI: 10.3390/molecules25102269 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.17 Å) |
Structure validation
Download full validation report
