6y9c
From Proteopedia
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==The structure of a quaternary ammonium Rieske monooxygenase reveals insights into carnitine oxidation by gut microbiota and inter-subunit electron transfer== | ==The structure of a quaternary ammonium Rieske monooxygenase reveals insights into carnitine oxidation by gut microbiota and inter-subunit electron transfer== | ||
| - | <StructureSection load='6y9c' size='340' side='right'caption='[[6y9c]]' scene=''> | + | <StructureSection load='6y9c' size='340' side='right'caption='[[6y9c]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Y9C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6y9c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Y9C FirstGlance]. <br> |
| - | </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=6y9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y9c OCA], [https://pdbe.org/6y9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y9c RCSB], [https://www.ebi.ac.uk/pdbsum/6y9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y9c ProSAT]</span></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]] 1.8Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=152:CARNITINE'>152</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</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=6y9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y9c OCA], [https://pdbe.org/6y9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y9c RCSB], [https://www.ebi.ac.uk/pdbsum/6y9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y9c ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CNTA_ACIB2 CNTA_ACIB2] Converts carnitine to trimethylamine and malic semialdehyde.[HAMAP-Rule:MF_02097]<ref>PMID:24591617</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Rieske monooxygenases undertake complex catalysis integral to marine, terrestrial and human gut-ecosystems. Group-I to IV Rieske monooxygenases accept aromatic substrates and have well characterised catalytic mechanisms. Nascent to our understanding are Group-V members catalysing the oxidation/breakdown of quaternary ammonium substrates. Phylogenetic analysis of Group V highlights a cysteine residue-pair adjacent to the mononuclear Fe active site with no established role. Following our elucidation of the carnitine monooxygenase CntA structure, we probed the function of the cysteine pair Cys206/Cys209. Utilising biochemical and biophysical techniques, we found the cysteine residues do not play a structural role nor influence the electron transfer pathway, but rather are used in a non-stoichiometric role to ensure the catalytic iron centre remains in an Fe(II) state. | ||
| + | |||
| + | Characterisation of an unusual cysteine pair in the Rieske carnitine monooxygenase CntA catalytic site.,Quareshy M, Shanmugam M, Cameron AD, Bugg TDH, Chen Y FEBS J. 2023 Jan 8. doi: 10.1111/febs.16722. PMID:36617384<ref>PMID:36617384</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6y9c" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Acinetobacter baumannii]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bugg TD]] | [[Category: Bugg TD]] | ||
Current revision
The structure of a quaternary ammonium Rieske monooxygenase reveals insights into carnitine oxidation by gut microbiota and inter-subunit electron transfer
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