|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6qp3' size='340' side='right'caption='[[6qp3]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='6qp3' size='340' side='right'caption='[[6qp3]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6qp3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QP3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6QP3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6qp3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QP3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QP3 FirstGlance]. <br> |
| - | </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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6qp1|6qp1]], [[6qp2|6qp2]], [[6rvi|6rvi]], [[6rvj|6rvj]]</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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">patB, BSU31440 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</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=6qp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qp3 OCA], [https://pdbe.org/6qp3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qp3 RCSB], [https://www.ebi.ac.uk/pdbsum/6qp3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qp3 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/Cysteine-S-conjugate_beta-lyase Cysteine-S-conjugate beta-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.13 4.4.1.13] </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=6qp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qp3 OCA], [http://pdbe.org/6qp3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qp3 RCSB], [http://www.ebi.ac.uk/pdbsum/6qp3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qp3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CBL_BACSU CBL_BACSU]] Catalyzes the transformation of cystathionine to homocysteine. Also exhibits cysteine desulfhydrase activity in vitro, producing sulfide from cysteine. | + | [https://www.uniprot.org/uniprot/CBL_BACSU CBL_BACSU] Catalyzes the transformation of cystathionine to homocysteine. Also exhibits cysteine desulfhydrase activity in vitro, producing sulfide from cysteine. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 28: |
Line 26: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| - | [[Category: Cysteine-S-conjugate beta-lyase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hanai, S]] | + | [[Category: Hanai S]] |
| - | [[Category: Herman, R]] | + | [[Category: Herman R]] |
| - | [[Category: Rudden, M]] | + | [[Category: Rudden M]] |
| - | [[Category: Thomas, G H]] | + | [[Category: Thomas GH]] |
| - | [[Category: Wilkinson, A J]] | + | [[Category: Wilkinson AJ]] |
| - | [[Category: Cysteine-s-conjugate beta-lyase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Pyridoxal phosphate binding]]
| + | |
| Structural highlights
Function
CBL_BACSU Catalyzes the transformation of cystathionine to homocysteine. Also exhibits cysteine desulfhydrase activity in vitro, producing sulfide from cysteine.
Publication Abstract from PubMed
Body odour is a characteristic trait of Homo sapiens, however its role in human behaviour and evolution is poorly understood. Remarkably, body odour is linked to the presence of a few species of commensal microbes. Herein we discover a bacterial enzyme, limited to odour-forming staphylococci that are able to cleave odourless precursors of thioalcohols, the most pungent components of body odour. We demonstrated using phylogenetics, biochemistry and structural biology that this cysteine-thiol lyase (C-T lyase) is a PLP-dependent enzyme that moved horizontally into a unique monophyletic group of odour-forming staphylococci about 60 million years ago, and has subsequently tailored its enzymatic function to human-derived thioalcohol precursors. Significantly, transfer of this enzyme alone to non-odour producing staphylococci confers odour production, demonstrating that this C-T lyase is both necessary and sufficient for thioalcohol formation. The structure of the C-T lyase compared to that of other related enzymes reveals how the adaptation to thioalcohol precursors has evolved through changes in the binding site to create a constrained hydrophobic pocket that is selective for branched aliphatic thioalcohol ligands. The ancestral acquisition of this enzyme, and the subsequent evolution of the specificity for thioalcohol precursors implies that body odour production in humans is an ancient process.
The molecular basis of thioalcohol production in human body odour.,Rudden M, Herman R, Rose M, Bawdon D, Cox DS, Dodson E, Holden MTG, Wilkinson AJ, James AG, Thomas GH Sci Rep. 2020 Jul 27;10(1):12500. doi: 10.1038/s41598-020-68860-z. PMID:32719469[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rudden M, Herman R, Rose M, Bawdon D, Cox DS, Dodson E, Holden MTG, Wilkinson AJ, James AG, Thomas GH. The molecular basis of thioalcohol production in human body odour. Sci Rep. 2020 Jul 27;10(1):12500. doi: 10.1038/s41598-020-68860-z. PMID:32719469 doi:http://dx.doi.org/10.1038/s41598-020-68860-z
|
