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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
17
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pubmed:dateCreated |
2000-9-19
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pubmed:databankReference |
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pubmed:abstractText |
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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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-10089316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-10440379,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-10586886,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-15299354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-1538787,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-1758883,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-2025413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-2185834,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-2231712,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-369599,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-4333397,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-4575624,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-4579004,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-4582730,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-7552726,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-7578233,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-7578234,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-7630882,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-795808,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-8121489,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-8268803,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-8377180,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-8401235,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-8743695,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-8842196,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-8867839,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-8987983,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-9261083,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-9541386,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-9757093,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10944213-9757107
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
97
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9413-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10944213-Amino Acid Sequence,
pubmed-meshheading:10944213-Binding Sites,
pubmed-meshheading:10944213-Cell Membrane,
pubmed-meshheading:10944213-Cell Respiration,
pubmed-meshheading:10944213-Crystallography, X-Ray,
pubmed-meshheading:10944213-Escherichia coli,
pubmed-meshheading:10944213-Flavin-Adenine Dinucleotide,
pubmed-meshheading:10944213-L-Lactate Dehydrogenase,
pubmed-meshheading:10944213-Lactic Acid,
pubmed-meshheading:10944213-Membrane Proteins,
pubmed-meshheading:10944213-Models, Molecular,
pubmed-meshheading:10944213-Molecular Sequence Data,
pubmed-meshheading:10944213-Protein Binding,
pubmed-meshheading:10944213-Protein Structure, Secondary,
pubmed-meshheading:10944213-Protein Structure, Tertiary,
pubmed-meshheading:10944213-Sequence Alignment,
pubmed-meshheading:10944213-Static Electricity
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pubmed:year |
2000
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pubmed:articleTitle |
The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme.
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pubmed:affiliation |
Department of Energy Laboratory of Structural Biology and Molecular Medicine, University of California, Los Angeles 90095, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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