6mp9: Difference between revisions
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==X-ray crystal structure of VioC bound to Fe(II), 2-oxo-5-guanidinopentanoic acid, and succinate== | |||
<StructureSection load='6mp9' size='340' side='right'caption='[[6mp9]], [[Resolution|resolution]] 1.89Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6mp9]] 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=6MP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MP9 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]] 1.89Å</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=JX7:5-carbamimidamido-2-oxopentanoic+acid'>JX7</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=6mp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mp9 OCA], [https://pdbe.org/6mp9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mp9 RCSB], [https://www.ebi.ac.uk/pdbsum/6mp9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mp9 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: Boal | __TOC__ | ||
[[Category: Dunham | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Streptomyces vinaceus]] | |||
[[Category: Boal AK]] | |||
[[Category: Dunham NP]] | |||
Latest revision as of 17:44, 13 March 2024
X-ray crystal structure of VioC bound to Fe(II), 2-oxo-5-guanidinopentanoic acid, and succinateX-ray crystal structure of VioC bound to Fe(II), 2-oxo-5-guanidinopentanoic acid, and succinate
Structural highlights
FunctionARGHX_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.[1] [2] [3] See AlsoReferences
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