6y9c: Difference between revisions

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<StructureSection load='6y9c' size='340' side='right'caption='[[6y9c]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='6y9c' size='340' side='right'caption='[[6y9c]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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]] 1.8&#8491;</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='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>
<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>
From MEDLINE&reg;/PubMed&reg;, 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]]

Latest revision as of 18:43, 8 September 2026

The structure of a quaternary ammonium Rieske monooxygenase reveals insights into carnitine oxidation by gut microbiota and inter-subunit electron transfer

6y9c, resolution 1.80Å

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