2g1h

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[[Image:2g1h.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_2g1h| PDB=2g1h | SCENE= }}
{{STRUCTURE_2g1h| PDB=2g1h | SCENE= }}
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'''Structure of E.coli FabD complexed with glycerol'''
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===Structure of E.coli FabD complexed with glycerol===
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==Overview==
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Malonyl-CoA-acyl carrier protein transacylase (FabD; EC 2.3.1.39) is a key enzyme in the fatty-acid biosynthesis pathway of bacteria, catalyzing the transfer of a malonyl moiety from malonyl-CoA to holo acyl carrier protein (ACP), generating malonyl-ACP and free CoASH. Malonyl-ACP, which is the product of this reaction, is the key building block for de novo fatty-acid biosynthesis. Various binary complex structures of the Escherichia coli enzyme are presented, including that of the natural substrate malonyl-CoA, indicating the functional role of the highly conserved amino acids Gln11, Ser92, Arg117 and His201 and the stabilizing function of the preformed oxyanion hole during the enzymatic reaction. Based on the presented structural data, a possible new catalytic enzyme mechanism is discussed. The data obtained could be used in aiding the process of rational inhibitor design.
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(as it appears on PubMed at http://www.pubmed.gov), where 16699188 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16699188}}
==About this Structure==
==About this Structure==
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[[Category: Oefner, C.]]
[[Category: Oefner, C.]]
[[Category: Complex]]
[[Category: Complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:35:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:11:49 2008''

Revision as of 13:11, 29 July 2008

Image:2g1h.png

Template:STRUCTURE 2g1h

Structure of E.coli FabD complexed with glycerol

Template:ABSTRACT PUBMED 16699188

About this Structure

2G1H is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Mapping the active site of Escherichia coli malonyl-CoA-acyl carrier protein transacylase (FabD) by protein crystallography., Oefner C, Schulz H, D'Arcy A, Dale GE, Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):613-8. Epub 2006, May 12. PMID:16699188

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