6ssd
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Transaminase with PLP bound== | |
| + | <StructureSection load='6ssd' size='340' side='right'caption='[[6ssd]], [[Resolution|resolution]] 1.18Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6ssd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_kaniharaensis Streptomyces kaniharaensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SSD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SSD 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]] 1.18Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6ssd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ssd OCA], [https://pdbe.org/6ssd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ssd RCSB], [https://www.ebi.ac.uk/pdbsum/6ssd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ssd ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A6I8WFW1_9ACTN A0A6I8WFW1_9ACTN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | ForI is a PLP-dependent enzyme from the biosynthetic pathway of the C-nucleoside antibiotic formycin. Cycloserine is thought to inhibit PLP-dependent enzymes by irreversibly forming a PMP-isoxazole. We now report that ForI forms novel PMP-diketopiperazine derivatives following incubation with both d and l cycloserine. This unexpected result suggests chemical diversity in the chemistry of cycloserine inhibition. | ||
| - | + | PMP-diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis.,Gao S, Liu H, de Crecy-Lagard V, Zhu W, Richards NGJ, Naismith JH Chem Commun (Camb). 2019 Nov 28;55(96):14502-14505. doi: 10.1039/c9cc06975e. PMID:31730149<ref>PMID:31730149</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6ssd" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces kaniharaensis]] | ||
| + | [[Category: Gao S]] | ||
| + | [[Category: Naismith JH]] | ||
Current revision
Transaminase with PLP bound
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