6c3d: Difference between revisions
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==O2-, PLP-dependent L-arginine hydroxylase RohP quinonoid II complex== | |||
<StructureSection load='6c3d' size='340' side='right'caption='[[6c3d]], [[Resolution|resolution]] 1.55Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6c3d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_cattleya_NRRL_8057_=_DSM_46488 Streptomyces cattleya NRRL 8057 = DSM 46488]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6C3D 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]] 1.55Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EMS:(2E,3E)-5-carbamimidamido-2-{[(Z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1H)-ylidene}methyl]imino}pent-3-enoic+acid'>EMS</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=6c3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c3d OCA], [https://pdbe.org/6c3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6c3d RCSB], [https://www.ebi.ac.uk/pdbsum/6c3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6c3d ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/G8WNK6_STREN G8WNK6_STREN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Enzymes that catalyze hydroxylation of unactivated carbons normally contain heme and nonheme iron cofactors. By contrast, how a pyridoxal phosphate (PLP)-dependent enzyme could catalyze such a hydroxylation was unknown. Here, we investigate RohP, a PLP-dependent enzyme that converts l-arginine to (S)-4-hydroxy-2-ketoarginine. We determine that the RohP reaction consumes oxygen with stoichiometric release of H2O2. To understand this unusual chemistry, we obtain approximately 1.5 A resolution structures that capture intermediates along the catalytic cycle. Our data suggest that RohP carries out a four-electron oxidation and a stereospecific alkene hydration to give the (S)-configured product. Together with our earlier studies on an O2, PLP-dependent l-arginine oxidase, our work suggests that there is a shared pathway leading to both oxidized and hydroxylated products from l-arginine. | |||
Snapshots of the Catalytic Cycle of an O2, Pyridoxal Phosphate-Dependent Hydroxylase.,Hedges JB, Kuatsjah E, Du YL, Eltis LD, Ryan KS ACS Chem Biol. 2018 Feb 28. doi: 10.1021/acschembio.8b00039. PMID:29466666<ref>PMID:29466666</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6c3d" style="background-color:#fffaf0;"></div> | ||
[[Category: Hedges | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces cattleya NRRL 8057 = DSM 46488]] | |||
[[Category: Hedges JB]] | |||
[[Category: Ryan KS]] | |||
Latest revision as of 14:55, 4 October 2023
O2-, PLP-dependent L-arginine hydroxylase RohP quinonoid II complex
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