6mp8: Difference between revisions

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OCA

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-'''Unreleased structure'''
-The entry 6mp8 is ON HOLD  until Paper Publication
+==X-ray crystal structure of VioC bound to Fe(II), D-arginine, and 2-oxoglutarate==
+<StructureSection load='6mp8' size='340' side='right'caption='[[6mp8]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6mp8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_vinaceus Streptomyces vinaceus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MP8 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]] 1.89&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=DAR:D-ARGININE'>DAR</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</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=6mp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mp8 OCA], [https://pdbe.org/6mp8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mp8 RCSB], [https://www.ebi.ac.uk/pdbsum/6mp8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mp8 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ARGHX_STRVI ARGHX_STRVI] Involved in the biosynthesis of capreomycidine, an unusual amino acid used by non-ribosomal peptide synthases (NRPS) to make the tuberactinomycin class of peptide antibiotics such as viomycin and capreomycin. Catalyzes the stereospecific hydroxylation of the C3 of (2S)-arginine to generate (3S)-hydroxy-(2S)-arginine. Usually clavaminic acid synthase-like oxygenases catalyze the formation of threo diastereomers, however VioC produces the erythro diastereomer of beta-carbon-hydroxylated L-arginine. It exerts a broad substrate specificity by accepting the analogs L-homoarginine and L-canavanine for the beta-carbon hydroxylation.<ref>PMID:15368580</ref> <ref>PMID:15368582</ref> <ref>PMID:19490124</ref>
-Authors: Dunham, N.P., Boal, A.K.
+==See Also==
+*[[Hydroxylases 3D structures|Hydroxylases 3D structures]]
-Description: X-ray crystal structure of VioC bound to Fe(II), D-arginine, and 2-oxoglutarate
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
-[[Category: Boal, A.K]]
+__TOC__
-[[Category: Dunham, N.P]]
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Streptomyces vinaceus]]
+[[Category: Boal AK]]
+[[Category: Dunham NP]]