3b9g

Crystal structure of loop deletion mutant of Trypanosoma vivax nucleoside hydrolase (3GTvNH) in complex with ImmH

spinqualitylabelsall models 3b9g, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3b9g is a 2 chain structure with sequence from Trypanosoma vivax. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, IMH, NA Related: 1hoz, 1hpo, 1kic, 1kie, 1r4f, 2mas Activity: Purine nucleosidase, with EC number 3.2.2.1 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The nucleoside hydrolase of Trypanosoma vivax hydrolyzes the N-glycosidic bond of purine nucleosides. Structural and kinetic studies on this enzyme have suggested a catalytic role for a flexible loop in the vicinity of the active sites. Here we present the analysis of the role of this flexible loop via the combination of a proline scan of the loop, loop deletion mutagenesis, steady state and pre-steady state analysis, and x-ray crystallography. Our analysis reveals that this loop has an important role in leaving group activation and product release. The catalytic role involves the entire loop and could only be perturbed by deletion of the entire loop and not by single site mutagenesis. We present evidence that the loop closes over the active site during catalysis, thereby ordering a water channel that is involved in leaving group activation. Once chemistry has taken place, the loop dynamics determine the rate of product release. A flexible loop as a functional element in the catalytic mechanism of nucleoside hydrolase from Trypanosoma vivax.,Vandemeulebroucke A, De Vos S, Van Holsbeke E, Steyaert J, Versees W J Biol Chem. 2008 Aug 8;283(32):22272-82. Epub 2008 Jun 2. PMID:18519562 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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