1f0x
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CRYSTAL STRUCTURE OF D-LACTATE DEHYDROGENASE, A PERIPHERAL MEMBRANE RESPIRATORY ENZYME.
OverviewOverview
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.
About this StructureAbout this Structure
1F0X is a Single protein structure of sequence from Escherichia coli with FAD as ligand. Active as D-lactate dehydrogenase, with EC number 1.1.1.28 Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme., Dym O, Pratt EA, Ho C, Eisenberg D, Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9413-8. PMID:10944213
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