Abstract
The crystal structure of D-lactate dehydrogenase from Aquifex aeolicus (aq_727) was determined to 2.12 A resolution in space group P2(1)2(1)2(1), with unit-cell parameters a = 90.94, b = 94.43, c = 188.85 A. The structure was solved by molecular replacement using the coenzyme-binding domain of Lactobacillus helveticus D-lactate dehydrogenase and contained two homodimers in the asymmetric unit. Each subunit of the homodimer was found to be in a ;closed' conformation with the NADH cofactor bound to the coenzyme-binding domain and with a lactate (or pyruvate) molecule bound at the interdomain active-site cleft.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacteria / enzymology*
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Bacteria / genetics
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Catalytic Domain
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Cloning, Molecular
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Crystallography, X-Ray
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Genes, Bacterial
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Lactate Dehydrogenases / chemistry*
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Lactate Dehydrogenases / genetics
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Lactic Acid / chemistry
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Lactobacillus helveticus / enzymology
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Models, Molecular
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NAD / chemistry
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Protein Conformation
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Protein Structure, Quaternary
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Protein Structure, Tertiary
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Protein Subunits
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Pyruvic Acid / chemistry
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Static Electricity
Substances
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Protein Subunits
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Recombinant Proteins
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NAD
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Lactic Acid
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Pyruvic Acid
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Lactate Dehydrogenases
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D-lactate dehydrogenase