1u6e
From Proteopedia
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|PDB= 1u6e |SIZE=350|CAPTION= <scene name='initialview01'>1u6e</scene>, resolution 1.85Å | |PDB= 1u6e |SIZE=350|CAPTION= <scene name='initialview01'>1u6e</scene>, resolution 1.85Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> |
| - | |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= fabH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]) | |GENE= fabH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1hzp|1HZP]], [[1ebl|1EBL]], [[1hnj|1HNJ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u6e OCA], [http://www.ebi.ac.uk/pdbsum/1u6e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u6e RCSB]</span> | ||
}} | }} | ||
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[[Category: Scarsdale, J N.]] | [[Category: Scarsdale, J N.]] | ||
[[Category: Wright, H T.]] | [[Category: Wright, H T.]] | ||
| - | [[Category: CL]] | ||
[[Category: 3-oxoacyl-[acyl-carrier-protein] synthase iii]] | [[Category: 3-oxoacyl-[acyl-carrier-protein] synthase iii]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:06:00 2008'' |
Revision as of 21:06, 30 March 2008
| |||||||
| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | fabH (Mycobacterium tuberculosis) | ||||||
| Activity: | Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 | ||||||
| Related: | 1HZP, 1EBL, 1HNJ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
1.85 Angstrom Crystal Structure of the C112A Mutant of Mycobacterium Tuberculosis Beta-Ketoacyl-Acyl Carrier Protein Synthase III (FabH)
Overview
Beta-ketoacyl-acyl carrier protein synthase III (FabH) catalyzes a two step reaction that initiates the pathway of fatty acid biosynthesis in plants and bacteria. In Mycobacterium tuberculosis, FabH catalyzes extension of lauroyl, myristoyl and palmitoyl groups from which cell wall mycolic acids of the bacterium are formed. The first step of the reaction is an acyl group transfer from acyl-coenzyme A to the active-site cysteine of the enzyme; the second step is acyl chain extension by two carbon atoms through Claisen condensation with malonyl-acyl carrier protein. We have previously determined the crystal structure of a type II, dissociated M.tuberculosis FabH, which catalyzes extension of lauroyl, myristoyl and palmitoyl groups. Here we describe the first long-chain Michaelis substrate complex of a FabH, that of lauroyl-coenzyme A with a catalytically disabled Cys-->Ala mutant of M.tuberculosis FabH. An elongated channel extending from the mutated active-site cysteine defines the acyl group binding locus that confers unique acyl substrate specificity on M.tuberculosis FabH. CoA lies in a second channel, bound primarily through interactions of its nucleotide group at the enzyme surface. The apparent weak association of CoA in this complex may play a role in the binding and dissociation of long chain acyl-CoA substrates and products and poses questions pertinent to the mechanism of this enzyme.
About this Structure
1U6E is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
Crystal structure of a substrate complex of Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III (FabH) with lauroyl-coenzyme A., Musayev F, Sachdeva S, Scarsdale JN, Reynolds KA, Wright HT, J Mol Biol. 2005 Mar 11;346(5):1313-21. Epub 2005 Jan 20. PMID:15713483[[Category: 3-oxoacyl-[acyl-carrier-protein] synthase iii]]
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