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5ddw
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ddw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinoalloteichus_sp._WH1-2216-6 Actinoalloteichus sp. WH1-2216-6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DDW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DDW FirstGlance]. <br> | <table><tr><td colspan='2'>[[5ddw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinoalloteichus_sp._WH1-2216-6 Actinoalloteichus sp. WH1-2216-6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DDW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DDW FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5B6:[5-HYDROXY-4-({(E)-[(4-HYDROXY-2,2-BIPYRIDIN-6-YL)METHYLIDENE]AMINO}METHYL)-6-METHYLPYRIDIN-3-YL]METHYL+DIHYDROGEN+PHOSPHATE'>5B6</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5B6:[5-HYDROXY-4-({(E)-[(4-HYDROXY-2,2-BIPYRIDIN-6-YL)METHYLIDENE]AMINO}METHYL)-6-METHYLPYRIDIN-3-YL]METHYL+DIHYDROGEN+PHOSPHATE'>5B6</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5ddw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ddw OCA], [https://pdbe.org/5ddw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ddw RCSB], [https://www.ebi.ac.uk/pdbsum/5ddw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ddw ProSAT]</span></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=5ddw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ddw OCA], [https://pdbe.org/5ddw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ddw RCSB], [https://www.ebi.ac.uk/pdbsum/5ddw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ddw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/H8Y6N2_9PSEU H8Y6N2_9PSEU] | [https://www.uniprot.org/uniprot/H8Y6N2_9PSEU H8Y6N2_9PSEU] | ||
| - | <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 5ddw" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in complex with the PMP external aldimine adduct with Caerulomycin M
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