6pqw: Difference between revisions
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<StructureSection load='6pqw' size='340' side='right'caption='[[6pqw]], [[Resolution|resolution]] 1.68Å' scene=''> | <StructureSection load='6pqw' size='340' side='right'caption='[[6pqw]], [[Resolution|resolution]] 1.68Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6pqw]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6pqw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodopseudomonas_palustris_HaA2 Rhodopseudomonas palustris HaA2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PQW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PQW FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OVV:3-methylbenzoic+acid'>OVV</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.679Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OVV:3-methylbenzoic+acid'>OVV</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6pqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pqw OCA], [https://pdbe.org/6pqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pqw RCSB], [https://www.ebi.ac.uk/pdbsum/6pqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pqw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q2IU02_RHOP2 Q2IU02_RHOP2] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6pqw" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6pqw" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Rhodopseudomonas palustris HaA2]] | ||
[[Category: Bell | [[Category: Bell SG]] | ||
[[Category: Bruning | [[Category: Bruning JB]] | ||
[[Category: Podgorski | [[Category: Podgorski MN]] | ||
Latest revision as of 10:33, 11 October 2023
The crystal structure of 3-methylbenzoate-bound CYP199A4The crystal structure of 3-methylbenzoate-bound CYP199A4
Structural highlights
FunctionPublication Abstract from PubMedThe cytochrome P450 metalloenzyme (CYP) CYP199A4 from Rhodopseudomonas palustris HaA2 catalyzes the highly efficient oxidation of para-substituted benzoic acids. Here we determined crystal structures of CYP199A4, and the binding and turnover parameters, with different meta-substituted benzoic acids in order to establish which criteria are important for efficient catalysis. When compared to the para isomers, the meta-substituted benzoic acids were less efficiently oxidized. For example, 3-formylbenzoic acid was oxidized with lower activity than the equivalent para isomer and 3-methoxybenzoic acid did not undergo O-demethylation by CYP199A4. The structural data highlighted that the meta-substituted benzoic acids bound in the enzyme active site in a modified position with incomplete loss of the distal water ligand of the heme moiety. However, for both sets of isomers the meta- or para-substituent pointed towards, and was in close proximity, to the heme iron. The absence of oxidation activity with 3-methoxybenzoic acid was assigned to the observation that the CH bonds of this molecule point away from the heme iron. In contrast, in the para isomer they are in an ideal location for abstraction. These findings were confirmed by using the bulkier 3-ethoxybenzoic acid as a substrate which removed the water ligand and reoriented the meta-substituent so that the methylene hydrogens pointed towards the heme, enabling more efficient oxidation. Overall we show relatively small changes in substrate structure and position in the active site can have a dramatic effect on the activity. Investigation of the requirements for efficient and selective cytochrome P450 monooxygenase catalysis across different reactions.,Podgorski MN, Coleman T, Chao RR, De Voss JJ, Bruning JB, Bell SG J Inorg Biochem. 2019 Nov 13;203:110913. doi: 10.1016/j.jinorgbio.2019.110913. PMID:31759265[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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