1F0X

CRYSTAL STRUCTURE OF D-LACTATE DEHYDROGENASE, A PERIPHERAL MEMBRANE RESPIRATORY ENZYME.

Summary for 1F0X

• Entry DOI: 10.2210/pdb1f0x/pdb
• Descriptor: D-LACTATE DEHYDROGENASE, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane ; Peripheral membrane protein ; Cytoplasmic side : P06149
• Total number of polymer chains: 2
• Total formula weight: 130983.62

Authors

Dym, O.,Pratt, E.A.,Ho, C.,Eisenberg, D. (deposition date: 2000-05-17, release date: 2000-08-23, Last modification date: 2024-02-07)

Primary citation

Dym, O.,Pratt, E.A.,Ho, C.,Eisenberg, D.
The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme.
Proc.Natl.Acad.Sci.USA, 97:9413-9418, 2000

PubMed 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.

PubMed: 10944213
DOI: 10.1073/pnas.97.17.9413

Experimental method

X-RAY DIFFRACTION (1.9 Å)