1POX

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

Summary for 1POX

• Entry DOI: 10.2210/pdb1pox/pdb
• Descriptor: PYRUVATE OXIDASE, MAGNESIUM ION, SODIUM ION, ... (7 entities in total)
• Functional Keywords: oxidoreductase(oxygen as acceptor)
• Biological source: Lactobacillus plantarum
• Total number of polymer chains: 2
• Total formula weight: 131115.32

Authors

Muller, Y.A.,Schulz, G.E. (deposition date: 1993-11-09, release date: 1994-01-31, Last modification date: 2024-02-14)

Primary citation

Muller, Y.A.,Schumacher, G.,Rudolph, R.,Schulz, G.E.
The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from Lactobacillus plantarum.
J.Mol.Biol., 237:315-335, 1994

PubMed Abstract: 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.

PubMed: 8145244
DOI: 10.1006/jmbi.1994.1233

Experimental method

X-RAY DIFFRACTION (2.1 Å)