6dax: Difference between revisions
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New page: '''Unreleased structure''' The entry 6dax is ON HOLD Authors: Dunham, N.P., Mitchell, A.J., Boal, A.K. Description: X-ray crystal structure of VioC bound to Fe(II), L-homoarginine, and... |
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==X-ray crystal structure of VioC bound to Fe(II), L-homoarginine, and 2-oxoglutarate== | |||
<StructureSection load='6dax' size='340' side='right'caption='[[6dax]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6dax]] 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=6DAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DAX 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]] 1.7Å</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=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HRG:L-HOMOARGININE'>HRG</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=6dax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dax OCA], [https://pdbe.org/6dax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dax RCSB], [https://www.ebi.ac.uk/pdbsum/6dax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dax 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: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Streptomyces vinaceus]] | |||
[[Category: Boal AK]] | |||
[[Category: Dunham NP]] | |||
[[Category: Mitchell AJ]] | |||
Latest revision as of 14:33, 13 March 2024
X-ray crystal structure of VioC bound to Fe(II), L-homoarginine, and 2-oxoglutarate
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