1g5x
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Beta-ketoacyl-acyl-carrier-protein_synthase_I Beta-ketoacyl-acyl-carrier-protein synthase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-ketoacyl-acyl-carrier-protein_synthase_I Beta-ketoacyl-acyl-carrier-protein synthase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] </span> |
|GENE= FABB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= FABB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1fj4|1FJ4]], [[1fj8|1FJ8]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g5x OCA], [http://www.ebi.ac.uk/pdbsum/1g5x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g5x RCSB]</span> | ||
}} | }} | ||
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[[Category: gene duplication]] | [[Category: gene duplication]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:37:18 2008'' |
Revision as of 17:37, 30 March 2008
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| , resolution 2.45Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | FABB (Escherichia coli) | ||||||
| Activity: | Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 | ||||||
| Related: | 1FJ4, 1FJ8
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The Structure of Beta-Ketoacyl-[Acyl Carrier Protein] Synthase I
Overview
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.
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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