1hn9

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{{STRUCTURE_1hn9| PDB=1hn9 | SCENE= }}
{{STRUCTURE_1hn9| PDB=1hn9 | SCENE= }}
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'''CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III'''
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===CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III===
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==Overview==
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Beta-ketoacyl-acyl carrier protein synthase III (FabH), the most divergent member of the family of condensing enzymes, is a key catalyst in bacterial fatty acid biosynthesis and a promising target for novel antibiotics. We report here the crystal structures of FabH determined in the presence and absence of acetyl-CoA. These structures display a fold that is common for condensing enzymes. The observed acetylation of Cys(112) proves its catalytic role and clearly defines the primer binding pocket. Modeling based on a bound CoA molecule suggests catalytic roles for His(244) and Asn(274). The structures provide the molecular basis for FabH substrate specificity and reaction mechanism and are important for structure-based design of novel antibiotics.
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(as it appears on PubMed at http://www.pubmed.gov), where 10593943 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10593943}}
==About this Structure==
==About this Structure==
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[[Category: Smith, W W.]]
[[Category: Smith, W W.]]
[[Category: Fabh]]
[[Category: Fabh]]
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Revision as of 05:25, 1 July 2008

Image:1hn9.png

Template:STRUCTURE 1hn9

CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III

Template:ABSTRACT PUBMED 10593943

About this Structure

1HN9 is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1d9b. Full crystallographic information is available from OCA.

Reference

Crystal structure of beta-ketoacyl-acyl carrier protein synthase III. A key condensing enzyme in bacterial fatty acid biosynthesis., Qiu X, Janson CA, Konstantinidis AK, Nwagwu S, Silverman C, Smith WW, Khandekar S, Lonsdale J, Abdel-Meguid SS, J Biol Chem. 1999 Dec 17;274(51):36465-71. PMID:10593943

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