6slf

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<StructureSection load='6slf' size='340' side='right'caption='[[6slf]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='6slf' size='340' side='right'caption='[[6slf]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6slf]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SLF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SLF FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6slf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_striatum"_chester_1901 "bacterium striatum" chester 1901]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SLF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SLF FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LJ8:(2~{S})-5-azanyl-2-[[[(3~{S})-3-methyl-5-phenyl-pentyl]-oxidanyl-phosphoryl]methyl]-5-oxidanylidene-pentanoic+acid'>LJ8</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LJ8:(2~{S})-5-azanyl-2-[[[(3~{S})-3-methyl-5-phenyl-pentyl]-oxidanyl-phosphoryl]methyl]-5-oxidanylidene-pentanoic+acid'>LJ8</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<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=6slf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6slf OCA], [http://pdbe.org/6slf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6slf RCSB], [http://www.ebi.ac.uk/pdbsum/6slf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6slf ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">agaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=43770 "Bacterium striatum" Chester 1901])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6slf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6slf OCA], [http://pdbe.org/6slf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6slf RCSB], [http://www.ebi.ac.uk/pdbsum/6slf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6slf ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Human axillary odor is known to be formed upon the action of Corynebacteria sp. on odorless axilla secretions. The known axilla odor determinant 3-methyl-2-hexenoic acid was identified in hydrolyzed axilla secretions along with a chemically related compound, 3-hydroxy-3-methylhexanoic acid. The natural precursors of both these acids were purified from non-hydrolyzed axilla secretions. From liquid chromatography/mass spectrometry analysis, it appeared that the acids are covalently linked to a glutamine residue in fresh axilla secretions, and the corresponding conjugates were synthesized for confirmation. Bacterial isolates obtained from the human axilla and belonging to the Corynebacteria were found to release the acids from these odorless precursors in vitro. A Zn(2+)-dependent aminoacylase mediating this cleavage was purified from Corynebacterium striatum Ax20, and the corresponding gene agaA was cloned and heterologously expressed in Escherichia coli. The enzyme is highly specific for the glutamine residue but has a low specificity for the acyl part of the substrate. agaA is closely related to many genes coding for enzymes involved in the cleavage of N-terminal acyl and aryl substituents from amino acids. This is the first report of the structure elucidation of precursors for human body odorants and the isolation of the bacterial enzyme involved in their cleavage.
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Human body odour is dominated by the scent of specific odourants emanating from specialized glands in the axillary region. These specific odourants are produced by an intricate interplay between biochemical pathways in the host and odour-releasing enzymes present in commensal microorganisms of the axillary microbiome. Key biochemical steps for the release of highly odouriferous carboxylic acids and sulfur compounds have been elucidated over the past 15 years. Based on the profound molecular understanding and specific analytical methods developed, evolutionary questions could be asked for the first time with small population studies: (i) a genetic basis for body odour could be shown with a twin study, (ii) no effect of genes in the human leukocyte antigen complex on the pattern of odourant carboxylic acid was found, and (iii) loss of odour precursor secretion by a mutation in the ABCC11 gene could explain why a large fraction of the population in the Far East lack body odour formation. This review summarizes what is currently known at the molecular level on the biochemistry of the formation of key odourants in the human axilla. At the same time, we present for the first time the crystal structure of the Nalpha-acyl-aminoacylase, a key human odour-releasing enzyme, thus describing at the molecular level how bacteria on the skin surface have adapted their enzyme to the specific substrates secreted by the human host. This article is part of the Theo Murphy meeting issue 'Olfactory communication in humans'.
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A specific bacterial aminoacylase cleaves odorant precursors secreted in the human axilla.,Natsch A, Gfeller H, Gygax P, Schmid J, Acuna G J Biol Chem. 2003 Feb 21;278(8):5718-27. doi: 10.1074/jbc.M210142200. Epub 2002, Dec 4. PMID:12468539<ref>PMID:12468539</ref>
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The specific biochemistry of human axilla odour formation viewed in an evolutionary context.,Natsch A, Emter R Philos Trans R Soc Lond B Biol Sci. 2020 Jun 8;375(1800):20190269. doi:, 10.1098/rstb.2019.0269. Epub 2020 Apr 20. PMID:32306870<ref>PMID:32306870</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacterium striatum chester 1901]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Emter, R]]
[[Category: Emter, R]]

Revision as of 07:05, 29 April 2020

Nalpha-acylglutamine aminoacylase from Corynebacterium sp.releasing human axilla odorants co-crystallised with high affinity inhibitor

PDB ID 6slf

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