3BMZ
Violacein biosynthetic enzyme VioE
Summary for 3BMZ
| Entry DOI | 10.2210/pdb3bmz/pdb |
| Descriptor | Putative uncharacterized protein, TETRAETHYLENE GLYCOL, TRIETHYLENE GLYCOL, ... (4 entities in total) |
| Functional Keywords | violacein, biosynthetic protein |
| Biological source | Chromobacterium violaceum |
| Total number of polymer chains | 2 |
| Total formula weight | 46097.65 |
| Authors | Ryan, K.S.,Drennan, C.L. (deposition date: 2007-12-13, release date: 2008-01-01, Last modification date: 2024-02-21) |
| Primary citation | Ryan, K.S.,Balibar, C.J.,Turo, K.E.,Walsh, C.T.,Drennan, C.L. The Violacein Biosynthetic Enzyme VioE Shares a Fold with Lipoprotein Transporter Proteins J.Biol.Chem., 283:6467-6475, 2008 Cited by PubMed Abstract: 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. PubMed: 18171675DOI: 10.1074/jbc.M708573200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.21 Å) |
Structure validation
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