1f0x: Difference between revisions
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'''CRYSTAL STRUCTURE OF D-LACTATE DEHYDROGENASE, A PERIPHERAL MEMBRANE RESPIRATORY ENZYME.''' | {{Structure | ||
|PDB= 1f0x |SIZE=350|CAPTION= <scene name='initialview01'>1f0x</scene>, resolution 1.9Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF D-LACTATE DEHYDROGENASE, A PERIPHERAL MEMBRANE RESPIRATORY ENZYME.''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1F0X is a [ | 1F0X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F0X OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10944213 10944213] | ||
[[Category: D-lactate dehydrogenase]] | [[Category: D-lactate dehydrogenase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:02:55 2008'' | ||
Revision as of 09:02, 20 March 2008
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| 1f0x, resolution 1.9Å | |||||||||||||
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| Ligands: | FAD | ||||||||||||
| Activity: | D-lactate dehydrogenase, with EC number 1.1.1.28 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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