5g3u

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(New page: '''Unreleased structure''' The entry 5g3u is ON HOLD Authors: Krausze, J., Rabe, J., Moser, J. Description: The structure of the L-tryptophan oxidase VioA from Chromobacterium violaceu...)
Current revision (13:37, 26 July 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 5g3u is ON HOLD
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==The structure of the L-tryptophan oxidase VioA from Chromobacterium violaceum in complex with its inhibitor 2-(1H-indol-3-ylmethyl)prop-2- enoic acid==
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<StructureSection load='5g3u' size='340' side='right'caption='[[5g3u]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5g3u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chromobacterium_violaceum Chromobacterium violaceum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G3U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G3U FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.377&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=FDA:DIHYDROFLAVINE-ADENINE+DINUCLEOTIDE'>FDA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ITW:2-[(1H-INDOL-3-YL)METHYL]PROP-2-ENOIC+ACID'>ITW</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5g3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g3u OCA], [https://pdbe.org/5g3u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g3u RCSB], [https://www.ebi.ac.uk/pdbsum/5g3u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g3u ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/VIOA_CHRVO VIOA_CHRVO]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Violacein is a natural purple pigment of Chromobacterium violaceum with potential medical applications as antimicrobial, antiviral and anticancer drugs. The initial step of violacein biosynthesis is the oxidative conversion of L-tryptophan into the corresponding alpha-imine catalyzed by the flavoenzyme L-tryptophan oxidase (VioA). A substrate-related (3-(1H-indol-3-yl)-2-methylpropanoic acid, IAA) and a product-related (2-(1H-indol-3-ylmethyl)prop-2-enoic acid, IEA) competitive VioA inhibitor was synthesized for subsequent kinetic and X-ray crystallographic investigations. Structures of the binary VioA/FADH2 and of the ternary VioA/FADH2/IEA complex were resolved. VioA forms a `loosely associated` homodimer as indicated by small-angle X-ray scattering experiments. VioA belongs to the GR2 family of FAD-dependent oxidoreductases according to the structurally conserved cofactor binding domain. The substrate-binding domain of VioA is mainly responsible for the specific recognition of L-tryptophan. Other canonical amino acids were efficiently discriminated with a minor conversion of L-phenylalanine. Furthermore, 7-aza-tryptophan, 1-methyl-tryptophan, 5-methyl-tryptophan and 5-fluoro-tryptophan were efficient substrates of VioA. The ternary product-related VioA structure indicated involvement of protein domain movement during enzyme catalysis. Extensive structure-based mutagenesis in combination with enzyme kinetics (using L-tryptophan and substrate analogs) identified Arg64, Lys269 and Tyr309 as key catalytic residues of VioA. An increased enzyme activity of protein variant H163A in the presence of L-phenylalanine indicated a functional role of the residues in substrate-binding. The combined structural and mutational analyses lead to the detailed understanding of VioA substrate recognition. Related strategies for the in vivo synthesis of novel violacein derivatives are discussed.
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Authors: Krausze, J., Rabe, J., Moser, J.
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Biosynthesis of Violacein: Structure and Function of L-Tryptophan Oxidase VioA from Chromobacterium violaceum.,Fuller JJ, Ropke R, Krausze J, Rennhack KE, Daniel NP, Blankenfeldt W, Schulz S, Jahn D, Moser J J Biol Chem. 2016 Jul 27. pii: jbc.M116.741561. PMID:27466367<ref>PMID:27466367</ref>
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Description: The structure of the L-tryptophan oxidase VioA from Chromobacterium violaceum in complex with its inhibitor 2-(1H-indol-3-ylmethyl)prop-2-enoic acid
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Moser, J]]
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<div class="pdbe-citations 5g3u" style="background-color:#fffaf0;"></div>
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[[Category: Rabe, J]]
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== References ==
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[[Category: Krausze, J]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Chromobacterium violaceum]]
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[[Category: Large Structures]]
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[[Category: Krausze J]]
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[[Category: Moser J]]
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[[Category: Rabe J]]

Current revision

The structure of the L-tryptophan oxidase VioA from Chromobacterium violaceum in complex with its inhibitor 2-(1H-indol-3-ylmethyl)prop-2- enoic acid

PDB ID 5g3u

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