5evy | pdb_00005evy

Salicylate hydroxylase substrate complex

spinqualitylabelsall models 5evy, resolution 2.47Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5evy is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FAD, SAL Activity: Salicylate 1-monooxygenase, with EC number 1.14.13.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Publication Abstract from PubMed The X-ray crystal structure of a salicylate hydroxylase from Pseudomonas putida S-1 complexed with coenzyme FAD has been determined to a resolution of 2.5 A. Structural conservation with p- or m-hydroxybenzoate hydroxylase is very good throughout the topology, despite a low amino sequence identity of 20-40% between these three hydroxylases. Salicylate hydroxylase is composed of three distinct domains and includes FAD between domains I and II, which is accessible to solvent. In this study, which analyzes the tertiary structure of the enzyme, the unique reaction of salicylate, i.e. decarboxylative hydroxylation, and the structural roles of amino acids surrounding the substrate, are considered. The catalytic mechanism of decarboxylative hydroxylation of salicylate hydroxylase revealed by crystal structure analysis at 2.5 A resolution.,Uemura T, Kita A, Watanabe Y, Adachi M, Kuroki R, Morimoto Y Biochem Biophys Res Commun. 2015 Nov 23. pii: S0006-291X(15)30956-6. doi:, 10.1016/j.bbrc.2015.11.087. PMID:26616054 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA