5zbd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:27, 27 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='5zbd' size='340' side='right'caption='[[5zbd]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='5zbd' size='340' side='right'caption='[[5zbd]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5zbd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZBD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZBD FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5zbd]] 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=5ZBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZBD FirstGlance]. <br>
-
</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=TRP:TRYPTOPHAN'>TRP</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/7-chloro-L-tryptophan_oxidase 7-chloro-L-tryptophan oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.23 1.4.3.23] </span></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=TRP:TRYPTOPHAN'>TRP</scene></td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5zbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zbd OCA], [http://pdbe.org/5zbd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zbd RCSB], [http://www.ebi.ac.uk/pdbsum/5zbd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zbd ProSAT]</span></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=5zbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zbd OCA], [https://pdbe.org/5zbd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zbd RCSB], [https://www.ebi.ac.uk/pdbsum/5zbd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zbd ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/VIOA_CHRVO VIOA_CHRVO]
-
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 5zbd" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: 7-chloro-L-tryptophan oxidase]]
+
[[Category: Chromobacterium violaceum ATCC 12472]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Asano, Y]]
+
[[Category: Asano Y]]
-
[[Category: Kashiwagi, T]]
+
[[Category: Kashiwagi T]]
-
[[Category: Mizukoshi, T]]
+
[[Category: Mizukoshi T]]
-
[[Category: Okazaki, S]]
+
[[Category: Okazaki S]]
-
[[Category: Sugiki, M]]
+
[[Category: Sugiki M]]
-
[[Category: Tagami, U]]
+
[[Category: Tagami U]]
-
[[Category: Takahashi, K]]
+
[[Category: Takahashi K]]
-
[[Category: Tatsumi, M]]
+
[[Category: Tatsumi M]]
-
[[Category: Yamaguchi, H]]
+
[[Category: Yamaguchi H]]
-
[[Category: Oxidase]]
+
-
[[Category: Oxidoreductase]]
+

Current revision

Crystal structure of tryptophan oxidase (C395A mutant) from Chromobacterium violaceum

PDB ID 5zbd

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5zbd"
Personal tools