1f0x

<table><tr><td colspan='2'>[[1f0x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F0X FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-lactate_dehydrogenase D-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.28 1.1.1.28] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f0x OCA], [http://pdbe.org/1f0x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f0x RCSB], [http://www.ebi.ac.uk/pdbsum/1f0x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f0x ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/DLD_ECOLI DLD_ECOLI]] First component of the membrane-bound D-lactate oxidase, which is believed to play an important role in the energization of the active transport of a variety of sugars and amino acids.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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<ref>PMID:10944213</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1f0x" style="background-color:#fffaf0;"></div>

*[[Lactate Dehydrogenase|Lactate Dehydrogenase]]

[[Category: Bacillus coli migula 1895]]

[[Category: D-lactate dehydrogenase]]

[[Category: Dym, O]]

[[Category: Eisenberg, D]]

[[Category: Ho, C]]

[[Category: Pratt, E A]]

[[Category: Oxidoreductase]]