View source for 6jc9


==Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in complex with amino donor L-Gln==
<StructureSection load='6jc9' size='340' side='right'caption='[[6jc9]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6jc9]] 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=6JC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JC9 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]] 2.35&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GLN:GLUTAMINE'>GLN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=6jc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jc9 OCA], [https://pdbe.org/6jc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jc9 RCSB], [https://www.ebi.ac.uk/pdbsum/6jc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jc9 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6jc9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Actinoalloteichus sp. WH1-2216-6]]
[[Category: Large Structures]]
[[Category: Liu J]]
[[Category: Xu J]]