4x5s | pdb_00004x5s

The crystal structure of an alpha carbonic anhydrase from the extremophilic bacterium Sulfurihydrogenibium azorense.

spinqualitylabelsall models 4x5s, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4x5s is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AZM, PE8, ZN Activity: Carbonate dehydratase, with EC number 4.2.1.1 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Two thermostable alpha-carbonic anhydrases (alpha-CAs) isolated from thermophilic Sulfurihydrogenibium spp., namely SspCA (from S. yellowstonensis) and SazCA (from S. azorense), were shown in a previous work to possess interesting complementary properties. SspCA was shown to have an exceptional thermal stability, whereas SazCA demonstrated to be the most active alpha-CA known to date for the CO2 hydration reaction. Here we report the crystallographic structure of SazCA and the identification of the structural features responsible for its high catalytic activity, by comparing it with SspCA structure. These data are of relevance for the design of engineered proteins showing higher stability and catalytic activity than other alpha-CAs known to date. Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorense.,De Simone G, Monti SM, Alterio V, Buonanno M, De Luca V, Rossi M, Carginale V, Supuran CT, Capasso C, Di Fiore A Bioorg Med Chem Lett. 2015 May 1;25(9):2002-6. doi: 10.1016/j.bmcl.2015.02.068., Epub 2015 Mar 6. PMID:25817590 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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