3bmz

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{{STRUCTURE_3bmz| PDB=3bmz | SCENE= }}
{{STRUCTURE_3bmz| PDB=3bmz | SCENE= }}
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'''Violacein biosynthetic enzyme VioE'''
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===Violacein biosynthetic enzyme VioE===
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==Overview==
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VioE, an unusual enzyme with no characterized homologues, plays a key role in the biosynthesis of violacein, a purple pigment with antibacterial and cytotoxic properties. Without bound cofactors or metals, VioE, from the bacterium Chromobacterium violaceum, mediates a 1,2 shift of an indole ring and oxidative chemistry to generate prodeoxyviolacein, a precursor to violacein. Our 1.21 A resolution structure of VioE shows that the enzyme shares a core fold previously described for lipoprotein transporter proteins LolA and LolB. For both LolB and VioE, a bound polyethylene glycol molecule suggests the location of the binding and/or active site of the protein. Mutations of residues near the bound polyethylene glycol molecule in VioE have identified the active site and five residues important for binding or catalysis. This structural and mutagenesis study suggests that VioE acts as a catalytic chaperone, using a fold previously associated with lipoprotein transporters to catalyze the production of its prodeoxyviolacein product.
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==About this Structure==
==About this Structure==
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[[Category: Biosynthetic protein]]
[[Category: Biosynthetic protein]]
[[Category: Violacein]]
[[Category: Violacein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:55:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:12:26 2008''

Revision as of 17:12, 27 July 2008

Image:3bmz.png

Template:STRUCTURE 3bmz

Violacein biosynthetic enzyme VioE

Template:ABSTRACT PUBMED 18171675

About this Structure

3BMZ is a Single protein structure of sequence from Chromobacterium violaceum. Full crystallographic information is available from OCA.

Reference

The Violacein Biosynthetic Enzyme VioE Shares a Fold with Lipoprotein Transporter Proteins., Ryan KS, Balibar CJ, Turo KE, Walsh CT, Drennan CL, J Biol Chem. 2008 Mar 7;283(10):6467-75. Epub 2008 Jan 2. PMID:18171675

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