PMID:10944213
| Citation |
Dym, O, Pratt, EA, Ho, C and Eisenberg, D (2000) The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme. Proc. Natl. Acad. Sci. U.S.A. 97:9413-8 |
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| Abstract |
d-Lactate dehydrogenase (d-LDH) of Escherichia coli is a peripheral membrane respiratory enzyme involved in electron transfer, located on the cytoplasmic side of the inner membrane. d-LDH catalyzes the oxidation of d-lactate to pyruvate, which is coupled to transmembrane transport of amino acids and sugars. Here we describe the crystal structure at 1.9 A resolution of the three domains of d-LDH: the flavin adenine dinucleotide (FAD)-binding domain, the cap domain, and the membrane-binding domain. The FAD-binding domain contains the site of d-lactate reduction by a noncovalently bound FAD cofactor and has an overall fold similar to other members of a recently discovered FAD-containing family of proteins. This structural similarity extends to the cap domain as well. The most prominent difference between d-LDH and the other members of the FAD-containing family is the membrane-binding domain, which is either absent in some of these proteins or differs significantly. The d-LDH membrane-binding domain presents an electropositive surface with six Arg and five Lys residues, which presumably interacts with the negatively charged phospholipid head groups of the membrane. Thus, d-LDH appears to bind the membrane through electrostatic rather than hydrophobic forces. |
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| Keywords |
Amino Acid Sequence; Binding Sites; Cell Membrane/metabolism; Cell Respiration; Crystallography, X-Ray; Escherichia coli/enzymology; Flavin-Adenine Dinucleotide/metabolism; L-Lactate Dehydrogenase/chemistry; L-Lactate Dehydrogenase/metabolism; Lactic Acid/metabolism; Membrane Proteins/chemistry; Membrane Proteins/metabolism; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Alignment; Static Electricity |
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