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| | <StructureSection load='4etw' size='340' side='right'caption='[[4etw]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='4etw' size='340' side='right'caption='[[4etw]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4etw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"shigella_paradysenteriae"_weldin_1927 "shigella paradysenteriae" weldin 1927] and [http://en.wikipedia.org/wiki/Shif8 Shif8]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ETW FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bioH, SF3435, S4329 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 "Shigella paradysenteriae" Weldin 1927]), acpP, SFV_1114, SSON_1114 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=373384 SHIF8])</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> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pimelyl-[acyl-carrier_protein]_methyl_ester_esterase Pimelyl-[acyl-carrier protein] methyl ester esterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.85 3.1.1.85] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4etw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4etw OCA], [http://pdbe.org/4etw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4etw RCSB], [http://www.ebi.ac.uk/pdbsum/4etw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4etw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BIOH_SHIFL BIOH_SHIFL]] The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters.[HAMAP-Rule:MF_01260] [[http://www.uniprot.org/uniprot/ACP_SHIF8 ACP_SHIF8]] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217] | + | [https://www.uniprot.org/uniprot/BIOH_SHIFL BIOH_SHIFL] The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters.[HAMAP-Rule:MF_01260] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Shigella paradysenteriae weldin 1927]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Shif8]] | + | [[Category: Shigella flexneri]] |
| - | [[Category: Agarwal, V]] | + | [[Category: Shigella flexneri 5 str. 8401]] |
| - | [[Category: Nair, S K]] | + | [[Category: Agarwal V]] |
| - | [[Category: Esterase]] | + | [[Category: Nair SK]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
BIOH_SHIFL The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters.[HAMAP-Rule:MF_01260]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Agarwal V, Lin S, Lukk T, Nair SK, Cronan JE. Structure of the enzyme-acyl carrier protein (ACP) substrate gatekeeper complex required for biotin synthesis. 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 doi:http://dx.doi.org/10.1073/pnas.1207028109
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