4etw: Difference between revisions
New page: '''Unreleased structure''' The entry 4etw is ON HOLD Authors: Agarwal, V, Nair, SK Description: Structure of the Enzyme-ACP Substrate Gatekeeper Complex Required for Biotin Synthesis |
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The | ==Structure of the Enzyme-ACP Substrate Gatekeeper Complex Required for Biotin Synthesis== | ||
<StructureSection load='4etw' size='340' side='right'caption='[[4etw]], [[Resolution|resolution]] 2.05Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4etw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri] and [https://en.wikipedia.org/wiki/Shigella_flexneri_5_str._8401 Shigella flexneri 5 str. 8401]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ETW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ETW FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZMK:METHYL+7-{[2-({N-[(2S)-2-HYDROXY-3,3-DIMETHYL-4-(PHOSPHONOOXY)BUTANOYL]-BETA-ALANYL}AMINO)ETHYL]SULFANYL}-7-OXOHEPTANOATE'>ZMK</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4etw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4etw OCA], [https://pdbe.org/4etw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4etw RCSB], [https://www.ebi.ac.uk/pdbsum/4etw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4etw ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ACP_SHIF8 ACP_SHIF8] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Although the pimeloyl moiety was long known to be a biotin precursor, the mechanism of assembly of this C7 alpha,omega-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-A 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. | |||
Structure of the enzyme-acyl carrier protein (ACP) substrate gatekeeper complex required for biotin synthesis.,Agarwal V, Lin S, Lukk T, Nair SK, Cronan JE Proc Natl Acad Sci U S A. 2012 Oct 23;109(43):17406-11. doi:, 10.1073/pnas.1207028109. Epub 2012 Oct 8. PMID:23045647<ref>PMID:23045647</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4etw" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Acyl carrier protein 3D structures|Acyl carrier protein 3D structures]] | |||
*[[Beta-ketoacyl carrier protein reductase 3D structures|Beta-ketoacyl carrier protein reductase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Shigella flexneri]] | |||
[[Category: Shigella flexneri 5 str. 8401]] | |||
[[Category: Agarwal V]] | |||
[[Category: Nair SK]] | |||
Latest revision as of 12:58, 30 October 2024
Structure of the Enzyme-ACP Substrate Gatekeeper Complex Required for Biotin SynthesisStructure of the Enzyme-ACP Substrate Gatekeeper Complex Required for Biotin Synthesis
Structural highlights
FunctionACP_SHIF8 Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217] Publication Abstract from PubMedAlthough the pimeloyl moiety was long known to be a biotin precursor, the mechanism of assembly of this C7 alpha,omega-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-A 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. Structure of the enzyme-acyl carrier protein (ACP) substrate gatekeeper complex required for biotin synthesis.,Agarwal V, Lin S, Lukk T, Nair SK, Cronan JE Proc Natl Acad Sci U S A. 2012 Oct 23;109(43):17406-11. doi:, 10.1073/pnas.1207028109. Epub 2012 Oct 8. PMID:23045647[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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