6k5e
From Proteopedia
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<StructureSection load='6k5e' size='340' side='right'caption='[[6k5e]], [[Resolution|resolution]] 2.26Å' scene=''> | <StructureSection load='6k5e' size='340' side='right'caption='[[6k5e]], [[Resolution|resolution]] 2.26Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6k5e]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K5E OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[6k5e]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pneumoniae"_(schroeter_1886)_flugge_1886 "bacillus pneumoniae" (schroeter 1886) flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K5E OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6K5E FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bioH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=573 "Bacillus pneumoniae" (Schroeter 1886) Flugge 1886])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | <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://proteopedia.org/fgij/fg.htm?mol=6k5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k5e OCA], [http://pdbe.org/6k5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k5e RCSB], [http://www.ebi.ac.uk/pdbsum/6k5e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k5e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/A0A0S4G6Z4_KLEPN A0A0S4G6Z4_KLEPN]] 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][SAAS:SAAS00186858] | [[http://www.uniprot.org/uniprot/A0A0S4G6Z4_KLEPN A0A0S4G6Z4_KLEPN]] 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][SAAS:SAAS00186858] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The BioH carboxylesterase which is a typical alpha/beta-hydrolase enzyme involved in biotin synthetic pathway in most bacteria. BioH acts as a gatekeeper and blocks the further elongation of its substrate. In the pathogen Klebsiella pneumoniae, BioH plays a critical role in the biosynthesis of biotin. To better understand the molecular function of BioH, we determined the crystal structure of BioH from K. pneumoniae at 2.26A resolution using X-ray crystallography. The structure of KpBioH consists of an alpha-beta-alpha sandwich domain and a cap domain. B-factor analysis revealed that the alpha-beta-alpha sandwich domain is a rigid structure, while the loops in the cap domain shows the structural flexibility. The active site of KpBioH contains the catalytic triad (Ser82-Asp207-His235) on the interface of the alpha-beta-alpha sandwich domain, which is surrounded by the cap domain. Size exclusion chromatography shows that KpBioH prefers the monomeric state in solution, whereas two-fold symmetric dimeric formation of KpBioH was observed in the asymmetric unit, the conserved Cys31-based disulfide bonds can maintain the irreversible dimeric formation of KpBioH. Our study provides important structural insight for understanding the molecular mechanisms of KpBioH and its homologous proteins. | ||
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| + | Structural insight into the carboxylesterase BioH from Klebsiella pneumoniae.,Wang L, Chen Y, Shang F, Liu W, Lan J, Gao P, Ha NC, Nam KH, Dong Y, Quan C, Xu Y Biochem Biophys Res Commun. 2019 Dec 10;520(3):538-543. doi:, 10.1016/j.bbrc.2019.10.050. Epub 2019 Oct 12. PMID:31615653<ref>PMID:31615653</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6k5e" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:25, 6 May 2020
Crystal structure of BioH from Klebsiella pneumonia
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