1f0x: Difference between revisions
New page: left|200px<br /><applet load="1f0x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f0x, resolution 1.9Å" /> '''CRYSTAL STRUCTURE OF ... |
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[[Image:1f0x.jpg|left|200px]]<br /><applet load="1f0x" size=" | [[Image:1f0x.jpg|left|200px]]<br /><applet load="1f0x" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1f0x, resolution 1.9Å" /> | caption="1f0x, resolution 1.9Å" /> | ||
'''CRYSTAL STRUCTURE OF D-LACTATE DEHYDROGENASE, A PERIPHERAL MEMBRANE RESPIRATORY ENZYME.'''<br /> | '''CRYSTAL STRUCTURE OF D-LACTATE DEHYDROGENASE, A PERIPHERAL MEMBRANE RESPIRATORY ENZYME.'''<br /> | ||
==Overview== | ==Overview== | ||
d-Lactate dehydrogenase (d-LDH) of Escherichia coli is a peripheral | 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== | ==About this Structure== | ||
1F0X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with FAD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | 1F0X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F0X OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Eisenberg, D.]] | [[Category: Eisenberg, D.]] | ||
[[Category: Ho, C.]] | [[Category: Ho, C.]] | ||
[[Category: Pratt, E | [[Category: Pratt, E A.]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:50 2008'' | ||
Revision as of 10:33, 21 February 2008
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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 with FAD as ligand. Active as D-lactate dehydrogenase, with EC number 1.1.1.28 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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