8dr2

Crystal structure of Neisseria gonorrhoeae carbonic anhydrase with 2-cyclohexyl-N-(5-sulfamoyl-1,3,4-thiadiazol-2-yl)acetamide

spinqualitylabelsall models 8dr2, resolution 2.81Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8dr2 is a 4 chain structure with sequence from Neisseria gonorrhoeae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.81Å Ligands: SO4, TE3, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CAH_NEIGO Reversible hydration of carbon dioxide. Publication Abstract from PubMed Drug-resistant Neisseria gonorrhoeae is a critical threat to public health, and bacterial carbonic anhydrases expressed by N. gonorrhoeae are potential new therapeutic targets to combat this pathogen. To further expand upon our recent reports of bacterial carbonic anhydrase inhibitors for the treatment of N. gonorrhoeae, our team has solved ligand-bound crystal structures of the FDA-approved carbonic anhydrase inhibitor acetazolamide, along with three analogs, in complex with the essential alpha-carbonic anhydrase isoform from N. gonorrhoeae. The structural data for the analogs presented bound to N. gonorrhoeae alpha-carbonic anhydrase supports the observed structure-activity relationship for in vitro inhibition with this scaffold against the enzyme. Moreover, the ligand-bound structures indicate differences in binding poses compared to those traditionally observed with the close human ortholog carbonic anhydrase II. These results present key differences in inhibitor binding between N. gonorrhoeae alpha-carbonic anhydrase and the human carbonic anhydrase II isoform. Structural Characterization of Thiadiazolesulfonamide Inhibitors Bound to Neisseria gonorrhoeae alpha-Carbonic Anhydrase.,Marapaka AK, Nocentini A, Youse MS, An W, Holly KJ, Das C, Yadav R, Seleem MN, Supuran CT, Flaherty DP ACS Med Chem Lett. 2022 Dec 6;14(1):103-109. doi: 10.1021/acsmedchemlett.2c00471. , eCollection 2023 Jan 12. PMID:36655133 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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