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6daz
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==X-ray crystal structure of VioC bound to Fe(II), 3S-hydroxy-L-homoarginine, and succinate== | |
| + | <StructureSection load='6daz' size='340' side='right'caption='[[6daz]], [[Resolution|resolution]] 1.94Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6daz]] 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=6DAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DAZ 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]] 1.94Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=G3M:(3S)-N~6~-carbamimidoyl-3-hydroxy-L-lysine'>G3M</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</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=6daz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6daz OCA], [https://pdbe.org/6daz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6daz RCSB], [https://www.ebi.ac.uk/pdbsum/6daz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6daz 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> | ||
| - | + | ==See Also== | |
| - | + | *[[Hydroxylases 3D structures|Hydroxylases 3D structures]] | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: Dunham | + | [[Category: Large Structures]] |
| + | [[Category: Streptomyces vinaceus]] | ||
| + | [[Category: Boal AK]] | ||
| + | [[Category: Dunham NP]] | ||
| + | [[Category: Mitchell AJ]] | ||
Current revision
X-ray crystal structure of VioC bound to Fe(II), 3S-hydroxy-L-homoarginine, and succinate
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