6yl7 | pdb_00006yl7

Crystal structure of beta carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomallei

spinqualitylabelsall models 6yl7, resolution 3.17Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6yl7 is a 1 chain structure with sequence from "bacillus_pseudomallei"_whitmore_1913 "bacillus pseudomallei" whitmore 1913. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Gene: can_1, can_2, BOC42_16450, CXQ84_19645, DF122_01465, ERS013345_01543, SAMEA1968934_03740 ("Bacillus pseudomallei" Whitmore 1913) Activity: Carbonate dehydratase, with EC number 4.2.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 beta-CA from Burkholderia pseudomallei was reported. The X-ray crystal structure of this new enzyme was solved at 2.7 A resolution, revealing a tetrameric type II beta-CA with a "closed" active site in which the zinc is tetrahedrally coordinated to Cys46, Asp48, His102, and Cys105. B. pseudomallei is known to encode at least two CAs, a beta-CA, and a gamma-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 beta-CA mechanism of action and the possibility to find selective inhibitors for this class of CAs. Crystal Structure of a Tetrameric Type II beta-Carbonic Anhydrase from the Pathogenic Bacterium Burkholderia pseudomallei.,Angeli A, Ferraroni M, Pinteala M, Maier SS, Simionescu BC, Carta F, Del Prete S, Capasso C, Supuran CT Molecules. 2020 May 12;25(10). pii: molecules25102269. doi:, 10.3390/molecules25102269. PMID:32408533 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Carbonic anhydrase 3D structures

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