1hn9
From Proteopedia
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'''CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III''' | '''CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HN9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry | + | 1HN9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1d9b 1d9b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Silverman, C.]] | [[Category: Silverman, C.]] | ||
[[Category: Smith, W W.]] | [[Category: Smith, W W.]] | ||
| - | [[Category: | + | [[Category: Fabh]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:02:00 2008'' | |
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Revision as of 16:02, 2 May 2008
CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III
Overview
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.
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 Page seeded by OCA on Fri May 2 19:02:00 2008
