1pox

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spinqualitylabelsall models 1pox, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

THE REFINED STRUCTURES OF A STABILIZED MUTANT AND OF WILD-TYPE PYRUVATE OXIDASE FROM LACTOBACILLUS PLANTARUM

Overview

The crystal structure of pyruvate oxidase (EC 1.2.3.3) from Lactobacillus, plantarum stabilized by three point mutations has been refined at 2.1 A, resolution using the simulated annealing method. Based on 87,775, independent reflections in the resolution range 10 to 2.1 A, a final, R-factor of 16.2% was obtained at good model geometry. The wild-type, enzyme crystallizes isomorphously with the stabilized enzyme and has been, analyzed at 2.5 A resolution. Pyruvate oxidase is a homotetramer with, point group symmetry D2. One 2-fold axis is crystallographic, the others, are local. The crystallographic asymmetric unit contains two subunits, and, the model consists of the two polypeptide chains (residues 9 through 593), two FAD, two ThDP*Mg2+ and 739 water molecules. Each subunit has three, domains; the CORE domain, the FAD domain and the ThDP domain. The, FAD-binding chain fold is different from those of other known, flavoproteins, whereas the ThDP-binding chain fold resembles the, corresponding folds of the two other ThDP enzymes whose structure is, known, transketolase and pyruvate decarboxylase. The peptide environment, most likely forces the pyrimidine ring of ThDP into an unusual tautomeric, form, which is required for catalysis. The structural differences between, the wild-type and the stabilized enzyme are small. All three point, mutations are at or near to the subunit interfaces, indicating that they, stabilize the quarternary structure as had been deduced from, reconstitution experiments.

About this Structure

1POX is a Single protein structure of sequence from Lactobacillus plantarum with MG, NA, TPP, FAD and GOL as ligands. Active as Pyruvate oxidase, with EC number 1.2.3.3 Full crystallographic information is available from OCA.

Reference

The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from Lactobacillus plantarum., Muller YA, Schumacher G, Rudolph R, Schulz GE, J Mol Biol. 1994 Apr 1;237(3):315-35. PMID:8145244

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