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5dds

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'''Unreleased structure'''
 
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The entry 5dds is ON HOLD until Paper Publication
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==Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in complex with PLP==
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<StructureSection load='5dds' size='340' side='right' caption='[[5dds]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5dds]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DDS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DDS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ddu|5ddu]], [[5ddw|5ddw]]</td></tr>
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<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=5dds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dds OCA], [http://pdbe.org/5dds PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dds RCSB], [http://www.ebi.ac.uk/pdbsum/5dds PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dds ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Xu, J., Feng, Z., Liu, J.
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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>
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Description: Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in complex with PLP
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Xu, J]]
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<div class="pdbe-citations 5dds" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Feng, Z]]
[[Category: Feng, Z]]
[[Category: Liu, J]]
[[Category: Liu, J]]
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[[Category: Xu, J]]
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[[Category: Aminotransferase]]
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[[Category: Caerulomycin some]]
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[[Category: Plp]]
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[[Category: Transferase]]

Revision as of 15:58, 10 August 2016

Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in complex with PLP

5dds, resolution 2.60Å

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