5ddw: 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]] 2.3&#8491;</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&reg;/PubMed&reg;, 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>

Latest revision as of 09:09, 20 March 2024

Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in complex with the PMP external aldimine adduct with Caerulomycin M

5ddw, resolution 2.30Å

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