View source for 5zbc


==Crystal structure of Se-Met tryptophan oxidase (C395A mutant) from Chromobacterium violaceum==
<StructureSection load='5zbc' size='340' side='right'caption='[[5zbc]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zbc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chromobacterium_violaceum_ATCC_12472 Chromobacterium violaceum ATCC 12472]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZBC 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5zbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zbc OCA], [https://pdbe.org/5zbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zbc RCSB], [https://www.ebi.ac.uk/pdbsum/5zbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zbc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VIOA_CHRVO VIOA_CHRVO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
l-Tryptophan oxidase, VioA from Chromobacterium violaceum, which has a high substrate specificity for tryptophan, is useful for quantitative assay of tryptophan. However, stability of wild type VioA is not enough for its application in clinical or industrial use. To improve the thermal stability of the enzyme, we developed a VioA (C395A) mutant, with higher stability than wild type VioA. The VioA (C395A) exhibited similar specificity and kinetic parameter for tryptophan to wild type. Conventionally, the quantity of tryptophan is determined by instrumental methods, such as high-performance liquid chromatography (HPLC) after pre-column-derivatization. Using the mutant enzyme, we succeeded in the tryptophan quantification in human plasma samples, to an accuracy of &lt;2.9% when compared to the instrumental method, and to a precision of CV &lt;3.2%. To analyse the improvement in storage stability and substrate specificity, we further determined the crystal structures of VioA (C395A) complexed with FAD, and with FAD and tryptophan at 1.8 A resolution.

Protein engineering for improving the thermostability of tryptophan oxidase and insights from structural analysis.,Yamaguchi H, Tatsumi M, Takahashi K, Tagami U, Sugiki M, Kashiwagi T, Kameya M, Okazaki S, Mizukoshi T, Asano Y J Biochem. 2018 Nov 1;164(5):359-367. doi: 10.1093/jb/mvy065. PMID:30053101<ref>PMID:30053101</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5zbc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chromobacterium violaceum ATCC 12472]]
[[Category: Large Structures]]
[[Category: Asano Y]]
[[Category: Kashiwagi T]]
[[Category: Mizukoshi T]]
[[Category: Okazaki S]]
[[Category: Sugiki M]]
[[Category: Tagami U]]
[[Category: Takahashi K]]
[[Category: Tatsumi M]]
[[Category: Yamaguchi H]]