6jcb
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in C2 space group== | |
| + | <StructureSection load='6jcb' size='340' side='right'caption='[[6jcb]], [[Resolution|resolution]] 2.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6jcb]] 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=6JCB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JCB 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]] 2.85Å</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=6jcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jcb OCA], [https://pdbe.org/6jcb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jcb RCSB], [https://www.ebi.ac.uk/pdbsum/6jcb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jcb ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/H8Y6N2_9PSEU H8Y6N2_9PSEU] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Amine compounds biosynthesis using omega-transaminases has received considerable attention in the pharmaceutical industry. However, the application of omega-transaminases was hampered by the fundamental challenge of severe by-product inhibition. Here, we report that omega-transaminase CrmG from Actinoalloteichus cyanogriseus WH1-2216-6 is insensitive to inhibition from by-product alpha-ketoglutarate or pyruvate. Combined with structural and QM/MM studies, we establish the detailed catalytic mechanism for CrmG. Our structural and biochemical studies reveal that the roof of the active site in PMP-bound CrmG is flexible, which will facilitate the PMP or by-product to dissociate from PMP-bound CrmG. Our results also show that amino acceptor caerulomycin M (CRM M), but not alpha-ketoglutarate or pyruvate, can form strong interactions with the roof of the active site in PMP-bound CrmG. Based on our results, we propose that the flexible roof of the active site in PMP-bound CrmG may facilitate CrmG to overcome inhibition from the by-product. | ||
| - | + | Structural studies reveal flexible roof of active site responsible for omega-transaminase CrmG overcoming by-product inhibition.,Xu J, Tang X, Zhu Y, Yu Z, Su K, Zhang Y, Dong Y, Zhu W, Zhang C, Wu R, Liu J Commun Biol. 2020 Aug 19;3(1):455. doi: 10.1038/s42003-020-01184-w. PMID:32814814<ref>PMID:32814814</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6jcb" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Actinoalloteichus sp. WH1-2216-6]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Liu J]] | ||
| + | [[Category: Xu J]] | ||
Current revision
Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in C2 space group
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