3bmz | pdb_00003bmz

Violacein biosynthetic enzyme VioE

spinqualitylabelsall models 3bmz, resolution 1.21Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3bmz is a 2 chain structure with sequence from Chromobacterium violaceum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PG4, PGE Gene: VioE (Chromobacterium violaceum) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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