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| - | [[Image:1pox.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1pox| PDB=1pox | SCENE= }} | | {{STRUCTURE_1pox| PDB=1pox | SCENE= }} |
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| - | '''THE REFINED STRUCTURES OF A STABILIZED MUTANT AND OF WILD-TYPE PYRUVATE OXIDASE FROM LACTOBACILLUS PLANTARUM'''
| + | ===THE REFINED STRUCTURES OF A STABILIZED MUTANT AND OF WILD-TYPE PYRUVATE OXIDASE FROM LACTOBACILLUS PLANTARUM=== |
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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_8145244}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8145244 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8145244}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Muller, Y A.]] | | [[Category: Muller, Y A.]] |
| | [[Category: Schulz, G E.]] | | [[Category: Schulz, G E.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:19:16 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:59:00 2008'' |
Revision as of 23:59, 27 July 2008
Template:STRUCTURE 1pox
THE REFINED STRUCTURES OF A STABILIZED MUTANT AND OF WILD-TYPE PYRUVATE OXIDASE FROM LACTOBACILLUS PLANTARUM
Template:ABSTRACT PUBMED 8145244
About this Structure
1POX is a Single protein structure of sequence from Lactobacillus plantarum. 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
Page seeded by OCA on Mon Jul 28 02:59:00 2008
