2g2y: Difference between revisions

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[[Image:2g2y.gif|left|200px]]
{{Seed}}
[[Image:2g2y.png|left|200px]]


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{{STRUCTURE_2g2y|  PDB=2g2y  |  SCENE=  }}  
{{STRUCTURE_2g2y|  PDB=2g2y  |  SCENE=  }}  


'''Structure of E.coli FabD complexed with malonate'''
===Structure of E.coli FabD complexed with malonate===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_16699188}}, adds the Publication Abstract to the page
(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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