Chem.283, Issue 10, 6467-6475, March 7, 2008 This Article All Versions of this Article: 283/10/6467 _most recent_ Services Google Scholar PubMed THE VIOLACEIN BIOSYNTHETIC ENZYME VIOE SHARES A FOLD WITH LIPOPROTEIN TRANSPORTER PROTEINS KATHERINE S.CARL J.KAITLYN E.CHRISTOPHER T.AND CATHERINE L.From the Department of Biology and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139 and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115 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.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.1.Structure of VioE shows that the enzyme shares a core fold previously described for lipoprotein transporter proteins LolA and LolB.Both LolB and VioE, a bound polyethylene glycol molecule suggests the location of the binding and/or active site of the protein.Of residues near the bound polyethylene glycol molecule in VioE have identified the active site and five residues important for binding or catalysis.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.Received for publication, October 16, 2007 , and in revised form, December 13, 2007._The atomic coordinates and structure factors (code 3BMZ) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ ().This work was supported in part by National Institutes of Health Grants GM65337 (to C.D.GM 20011 (to C.W.The MIT Center for Environmental Health Sciences NIEHS P30 ES002109.Work was also supported in part by National Science Foundation Grant 0070319, National Institutes of Health Grant GM68762, and other funds from the National Institutes of Health.Costs of publication of this article were defrayed in part by the payment of page charges.Must therefore be hereby marked "_advertisement_" in accordance with 18 U.Section 1734 solely to indicate this fact.On-line version of this article (available at ) contains supplemental Table S1 and supplemental Figs. 1 Supported by a Howard Hughes Medical Institute Predoctoral Fellowship.2 Supported by a National Science Foundation Graduate Research Fellowship.3 Supported by a Douglass College Science, Technology, Engineering, and Math Summer Research Experience Grant (Rutgers University) and Howard Hughes Medical Institute-MIT Summer Research Experience in Chemical Biology Grant 52005719.4 To whom correspondence should be addressed.Read more Effects and interactions in an environmentally relevant mixture of pharmaceuticals
Get more A pilot study of atomoxetine in young children with attention-deficit/hyperactivity disorder
