2qx1: Difference between revisions

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[[Image:2qx1.jpg|left|200px]]
{{Seed}}
[[Image:2qx1.png|left|200px]]


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{{STRUCTURE_2qx1|  PDB=2qx1  |  SCENE=  }}  
{{STRUCTURE_2qx1|  PDB=2qx1  |  SCENE=  }}  


'''Crystal structure of the complex between mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III (FABH) and decyl-COA disulfide'''
===Crystal structure of the complex between mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III (FABH) and decyl-COA disulfide===




==Overview==
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The dimeric Mycobacterium tuberculosis FabH (mtFabH) catalyses a Claisen-type condensation between an acyl-CoA and malonyl-acyl carrier protein (ACP) to initiate the Type II fatty acid synthase cycle. To analyze the initial covalent acylation of mtFabH with acyl-CoA, we challenged it with mixture of C(6)-C(20) acyl-CoAs and the ESI-MS analysis showed reaction at both subunits and a strict specificity for C(12) acyl CoA. Crystallographic and ESI-MS studies of mtFabH with a decyl-CoA disulfide inhibitor revealed a decyl chain bound in acyl-binding channels of both subunits through disulfide linkage to the active site cysteine. These data provide the first unequivocal evidence that both subunits of mtFabH can react with substrates or inhibitor. The discrepancy between the observed C(12) acyl-CoA substrate specificity in the initial acylation step and the higher catalytic efficiency of mtFabH for C(18)-C(20) acyl-CoA substrates in the overall mtFabH catalyzed reaction suggests a role for M. tuberculosis ACP as a specificity determinant in this reaction.
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{{ABSTRACT_PUBMED_18096200}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Probing reactivity and substrate specificity of both subunits of the dimeric Mycobacterium tuberculosis FabH using alkyl-CoA disulfide inhibitors and acyl-CoA substrates., Sachdeva S, Musayev F, Alhamadsheh MM, Neel Scarsdale J, Tonie Wright H, Reynolds KA, Bioorg Chem. 2008 Apr;36(2):85-90. Epub 2007 Dec 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18096200 18096200]
Probing reactivity and substrate specificity of both subunits of the dimeric Mycobacterium tuberculosis FabH using alkyl-CoA disulfide inhibitors and acyl-CoA substrates., Sachdeva S, Musayev F, Alhamadsheh MM, Neel Scarsdale J, Tonie Wright H, Reynolds KA, Bioorg Chem. 2008 Apr;36(2):85-90. Epub 2007 Dec 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18096200 18096200]
Crystal structure of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III., Scarsdale JN, Kazanina G, He X, Reynolds KA, Wright HT, J Biol Chem. 2001 Jun 8;276(23):20516-22. Epub 2001 Mar 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11278743 11278743]
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:[http://www.ncbi.nlm.nih.gov/pubmed/15713483 15713483]
[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: Structural basis for substrate specificity]]
[[Category: Structural basis for substrate specificity]]
[[Category: Transferase]]
[[Category: Transferase]]
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