View source for 6jix


==The cyrstal structure of taurine:2-oxoglutarate aminotransferase from Bifidobacterium kashiwanohense, in complex with PLP and glutamate==
<StructureSection load='6jix' size='340' side='right'caption='[[6jix]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6jix]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_kashiwanohense_PV20-2 Bifidobacterium kashiwanohense PV20-2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JIX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JIX 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]] 2.647&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</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=6jix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jix OCA], [https://pdbe.org/6jix PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jix RCSB], [https://www.ebi.ac.uk/pdbsum/6jix PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jix ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0A7I435_9BIFI A0A0A7I435_9BIFI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Taurine aminotransferases catalyze the first step in taurine catabolism in many taurine-degrading bacteria and play an important role in bacterial taurine metabolism in the mammalian gut. Here, we report the biochemical and structural characterization of a new taurine:2-oxoglutarate aminotransferase from the human gut bacterium Bifidobacterium kashiwanohense (BkToa). Biochemical assays revealed high specificity of BkToa for 2-oxoglutarate as the amine acceptor. The crystal structure of BkToa in complex with pyridoxal 5'-phosphate (PLP) and glutamate was determined at 2.7 A resolution. The enzyme forms a homodimer, with each monomer exhibiting a typical type I PLP-enzyme fold and conserved PLP-coordinating residues interacting with the PLP molecule. Two glutamate molecules are bound in sites near the predicted active site and they may occupy a path for substrate entry and product release. Molecular docking reveals a role for active site residues Trp21 and Arg156, conserved in Toa enzymes studied to date, in interacting with the sulfonate group of taurine. Bioinformatics analysis shows that the close homologs of BkToa are also present in other anaerobic gut bacteria.

Biochemical and structural investigation of taurine:2-oxoglutarate aminotransferase from Bifidobacterium kashiwanohense.,Li M, Wei Y, Yin J, Lin L, Zhou Y, Hua G, Cao P, Ang EL, Zhao H, Yuchi Z, Zhang Y Biochem J. 2019 Jun 11;476(11):1605-1619. doi: 10.1042/BCJ20190206. PMID:31088892<ref>PMID:31088892</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6jix" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bifidobacterium kashiwanohense PV20-2]]
[[Category: Large Structures]]
[[Category: Li M]]
[[Category: Lin L]]
[[Category: Yuchi Z]]
[[Category: Zhang Y]]