View source for 6c3a


==O2-, PLP-dependent L-arginine hydroxylase RohP 4-hydroxy-2-ketoarginine complex==
<StructureSection load='6c3a' size='340' side='right'caption='[[6c3a]], [[Resolution|resolution]] 1.53&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6c3a]] 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=6C3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6C3A 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]] 1.53&#8491;</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=EGV:(4S)-5-carbamimidamido-4-hydroxy-2-oxopentanoic+acid'>EGV</scene>, <scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</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=6c3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c3a OCA], [https://pdbe.org/6c3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6c3a RCSB], [https://www.ebi.ac.uk/pdbsum/6c3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6c3a 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6c3a" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces cattleya NRRL 8057 = DSM 46488]]
[[Category: Hedges JB]]
[[Category: Ryan KS]]