2xqz | pdb_00002xqz

NEUTRON STRUCTURE OF THE PERDEUTERATED TOHO-1 R274N R276N DOUBLE MUTANT BETA-LACTAMASE

spinqualitylabelsall models 2xqz, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xqz is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: DOD Related: 1iyp, 1we4, 2wyx, 1iys, 1iyo, 2xr0, 1bza, 1iyq Activity: Beta-lactamase, with EC number 3.5.2.6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BLT1_ECOLX] Has strong cefotaxime-hydrolyzing activity. Publication Abstract from PubMed Room temperature neutron diffraction data of the fully perdeuterated Toho-1 R274N/R276N double mutant beta-lactamase in the apo form were used to visualize deuterium atoms within the active site of the enzyme. This perdeuterated neutron structure of the Toho-1 R274N/R276N reveals the clearest picture yet of the ground-state active site protonation states and the complete hydrogen-bonding network in a beta-lactamase enzyme. The ground-state active site protonation states detailed in this neutron diffraction study are consistent with previous high-resolution X-ray studies that support the role of Glu166 as the general base during the acylation reaction in the class A beta-lactamase reaction pathway. The active site protonation states of perdeuterated Toho-1 beta-lactamase determined by neutron diffraction support a role for Glu166 as the general base in acylation.,Tomanicek SJ, Wang KK, Weiss KL, Blakeley MP, Cooper J, Chen Y, Coates L FEBS Lett. 2010 Dec 17. PMID:21168411 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-lactamase

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