2v8d | pdb_00002v8d
CRYSTAL STRUCTURE OF MUTANT E159A OF BETA-ALANINE SYNTHASE FROM SACCHAROMYCES KLUYVERI
|
Overview
beta-Alanine synthase is the final enzyme of the reductive pyrimidine, catabolic pathway, which is responsible for the breakdown of uracil and, thymine in higher organisms. The fold of the homodimeric enzyme from the, yeast Saccharomyces kluyveri identifies it as a member of the AcyI/M20, family of metallopeptidases. Its subunit consists of a catalytic domain, harboring a di-zinc center and a smaller dimerization domain. The present, site-directed mutagenesis studies identify Glu(159) and Arg(322) as, crucial for catalysis and His(262) and His(397) as functionally important, but not essential. We determined the crystal structures of wild-type, beta-alanine synthase in complex with the reaction product beta-alanine, and of the mutant E159A with the substrate N-carbamyl-beta-alanine, revealing the closed state of a dimeric AcyI/M20 metallopeptidase-like, enzyme. Subunit closure is achieved by a approximately 30 degrees rigid, body domain rotation, which completes the active site by integration of, substrate binding residues that belong to the dimerization domain of the, same or the partner subunit. Substrate binding is achieved via a salt, bridge, a number of hydrogen bonds, and coordination to one of the zinc, ions of the di-metal center.
About this Structure
2V8D is a Single protein structure of sequence from Lachancea kluyveri with ZN as ligand. Active as Beta-ureidopropionase, with EC number 3.5.1.6 Known structural/functional Sites: AC1, AC2, AC3 and AC4. Full crystallographic information is available from OCA.
Reference
Crystal structures of yeast -alanine synthase complexes reveal the mode of substrate binding and large scale domain closure movements., Lundgren S, Andersen B, Piskur J, Dobritzsch D, J Biol Chem. 2007 Dec 7;282(49):36037-47. Epub 2007 Oct 4. PMID:17916556
Page seeded by OCA on Sun Feb 3 10:50:24 2008
