4ETW
Structure of the Enzyme-ACP Substrate Gatekeeper Complex Required for Biotin Synthesis
Summary for 4ETW
| Entry DOI | 10.2210/pdb4etw/pdb |
| Descriptor | Pimelyl-[acyl-carrier protein] methyl ester esterase, Acyl carrier protein, methyl 7-{[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl]sulfanyl}-7-oxoheptanoate, ... (4 entities in total) |
| Functional Keywords | esterase, hydrolase |
| Biological source | Shigella flexneri More |
| Total number of polymer chains | 4 |
| Total formula weight | 77241.80 |
| Authors | Agarwal, V.,Nair, S.K. (deposition date: 2012-04-24, release date: 2012-10-17, Last modification date: 2024-10-30) |
| Primary citation | Agarwal, V.,Lin, S.,Lukk, T.,Nair, S.K.,Cronan, J.E. Structure of the enzyme-acyl carrier protein (ACP) substrate gatekeeper complex required for biotin synthesis. Proc.Natl.Acad.Sci.USA, 109:17406-17411, 2012 Cited by PubMed Abstract: Although the pimeloyl moiety was long known to be a biotin precursor, the mechanism of assembly of this C7 α,ω-dicarboxylic acid was only recently elucidated. In Escherichia coli, pimelate is made by bypassing the strict specificity of the fatty acid synthetic pathway. BioC methylates the free carboxyl of a malonyl thioester, which replaces the usual acetyl thioester primer. This atypical primer is transformed to pimeloyl-acyl carrier protein (ACP) methyl ester by two cycles of fatty acid synthesis. The question is, what stops this product from undergoing further elongation? Although BioH readily cleaves this product in vitro, the enzyme is nonspecific, which made assignment of its physiological substrate problematical, especially because another enzyme, BioF, could also perform this gatekeeping function. We report the 2.05-Å resolution cocrystal structure of a complex of BioH with pimeloyl-ACP methyl ester and use the structure to demonstrate that BioH is the gatekeeper and its physiological substrate is pimeloyl-ACP methyl ester. PubMed: 23045647DOI: 10.1073/pnas.1207028109 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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