| pubmed-article:10944213 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10944213 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:10944213 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:10944213 | lifeskim:mentions | umls-concept:C0112125 | lld:lifeskim |
| pubmed-article:10944213 | lifeskim:mentions | umls-concept:C0597391 | lld:lifeskim |
| pubmed-article:10944213 | lifeskim:mentions | umls-concept:C0205100 | lld:lifeskim |
| pubmed-article:10944213 | pubmed:issue | 17 | lld:pubmed |
| pubmed-article:10944213 | pubmed:dateCreated | 2000-9-19 | lld:pubmed |
| pubmed-article:10944213 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10944213 | 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. | lld:pubmed |
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| pubmed-article:10944213 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10944213 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10944213 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10944213 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10944213 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10944213 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:10944213 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:10944213 | pubmed:author | pubmed-author:EisenbergDD | lld:pubmed |
| pubmed-article:10944213 | pubmed:author | pubmed-author:HoCC | lld:pubmed |
| pubmed-article:10944213 | pubmed:author | pubmed-author:PrattE AEA | lld:pubmed |
| pubmed-article:10944213 | pubmed:author | pubmed-author:DyrJJ | lld:pubmed |
| pubmed-article:10944213 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10944213 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:10944213 | pubmed:volume | 97 | lld:pubmed |
| pubmed-article:10944213 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10944213 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10944213 | pubmed:pagination | 9413-8 | lld:pubmed |
| pubmed-article:10944213 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:10944213 | pubmed:meshHeading | pubmed-meshheading:10944213... | lld:pubmed |
| pubmed-article:10944213 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10944213 | pubmed:articleTitle | The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme. | lld:pubmed |
| pubmed-article:10944213 | pubmed:affiliation | Department of Energy Laboratory of Structural Biology and Molecular Medicine, University of California, Los Angeles 90095, USA. | lld:pubmed |
| pubmed-article:10944213 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10944213 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10944213 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:10944213 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| literatureCitation:126_1094... | literatureCitation:pubmed | pubmed-article:10944213 | lld:drugbank |
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