1g5x

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{{STRUCTURE_1g5x| PDB=1g5x | SCENE= }}
{{STRUCTURE_1g5x| PDB=1g5x | SCENE= }}
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'''The Structure of Beta-Ketoacyl-[Acyl Carrier Protein] Synthase I'''
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===The Structure of Beta-Ketoacyl-[Acyl Carrier Protein] Synthase I===
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==Overview==
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The molecular details that govern the specific interactions between acyl carrier protein (ACP) and the enzymes of fatty acid biosynthesis are unknown. We investigated the mechanism of ACP-protein interactions using a computational analysis to dock the NMR structure of ACP with the crystal structure of beta-ketoacyl-ACP synthase III (FabH) and experimentally tested the model by the biochemical analysis of FabH mutants. The activities of the mutants were assessed using both an ACP-dependent and an ACP-independent assay. The ACP interaction surface was defined by mutations that compromised FabH activity in the ACP-dependent assay but had no effect in the ACP-independent assay. ACP docked to a positively charged/hydrophobic patch adjacent to the active site tunnel on FabH, which included a conserved arginine (Arg-249) that was required for ACP docking. Kinetic analysis and direct binding studies between FabH and ACP confirmed the identification of Arg-249 as critical for FabH-ACP interaction. Our experiments reveal the significance of the positively charged/hydrophobic patch located adjacent to the active site cavities of the fatty acid biosynthesis enzymes and the high degree of sequence conservation in helix II of ACP across species.
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{{ABSTRACT_PUBMED_11078736}}
==About this Structure==
==About this Structure==
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[[Category: Enzyme]]
[[Category: Enzyme]]
[[Category: Gene duplication]]
[[Category: Gene duplication]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:10:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:29:38 2008''

Revision as of 01:29, 1 July 2008

Image:1g5x.png

Template:STRUCTURE 1g5x

The Structure of Beta-Ketoacyl-[Acyl Carrier Protein] Synthase I

Template:ABSTRACT PUBMED 11078736

About this Structure

1G5X is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Identification and analysis of the acyl carrier protein (ACP) docking site on beta-ketoacyl-ACP synthase III., Zhang YM, Rao MS, Heath RJ, Price AC, Olson AJ, Rock CO, White SW, J Biol Chem. 2001 Mar 16;276(11):8231-8. Epub 2000 Nov 14. PMID:11078736

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