1f0x

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[[Image:1f0x.jpg|left|200px]]
[[Image:1f0x.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1f0x |SIZE=350|CAPTION= <scene name='initialview01'>1f0x</scene>, resolution 1.9&Aring;
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The line below this paragraph, containing "STRUCTURE_1f0x", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1f0x| PDB=1f0x | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1f0x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f0x RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF D-LACTATE DEHYDROGENASE, A PERIPHERAL MEMBRANE RESPIRATORY ENZYME.'''
'''CRYSTAL STRUCTURE OF D-LACTATE DEHYDROGENASE, A PERIPHERAL MEMBRANE RESPIRATORY ENZYME.'''
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[[Category: Ho, C.]]
[[Category: Ho, C.]]
[[Category: Pratt, E A.]]
[[Category: Pratt, E A.]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:45:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:13:41 2008''
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Revision as of 12:45, 2 May 2008

Template:STRUCTURE 1f0x

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


Overview

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 Structure

1F0X is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 15:45:44 2008

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