5ddu
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in complex with PMP== | |
| + | <StructureSection load='5ddu' size='340' side='right' caption='[[5ddu]], [[Resolution|resolution]] 2.46Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ddu]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DDU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DDU FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ddw|5ddw]], [[5dds|5dds]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ddu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ddu OCA], [http://pdbe.org/5ddu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ddu RCSB], [http://www.ebi.ac.uk/pdbsum/5ddu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ddu ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Caerulomycin A (CRM A 1) belongs to a family of natural products containing a 2,2'-bipyridyl ring core structure and is currently under development as a potent novel immunosuppressive agent. Herein, we report the functional characterization, kinetic analysis, substrate specificity, and structure insights of an aminotransferase CrmG in 1 biosynthesis. The aminotransferase CrmG was confirmed to catalyze a key transamination reaction to convert an aldehyde group to an amino group in the 1 biosynthetic pathway, preferring l-glutamate and l-glutamine as the amino donor substrates. The crystal structures of CrmG in complex with the cofactor 5'-pyridoxal phosphate (PLP) or 5'-pyridoxamine phosphate (PMP) or the acceptor substrate were determined to adopt a canonical fold-type I of PLP-dependent enzymes with a unique small additional domain. The structure guided site-directed mutagenesis identified key amino acid residues for substrate binding and catalytic activities, thus providing insights into the transamination mechanism of CrmG. | ||
| - | + | Biochemical and Structural Insights into the Aminotransferase CrmG in Caerulomycin Biosynthesis.,Zhu Y, Xu J, Mei X, Feng Z, Zhang L, Zhang Q, Zhang G, Zhu W, Liu J, Zhang C ACS Chem Biol. 2016 Apr 15;11(4):943-52. doi: 10.1021/acschembio.5b00984. Epub, 2016 Jan 12. PMID:26714051<ref>PMID:26714051</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5ddu" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Feng, Z]] | [[Category: Feng, Z]] | ||
[[Category: Liu, J]] | [[Category: Liu, J]] | ||
| + | [[Category: Xu, J]] | ||
| + | [[Category: Aminotransferase]] | ||
| + | [[Category: Caerulomycin biosynthesis]] | ||
| + | [[Category: Plp]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 15:49, 10 August 2016
Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in complex with PMP
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