Crystal Structure of VioE, a Key Player in the Construction of the Molecular Skeleton of Violacein

Hirano, Seishiro; Asamizu, Shumpei; Onaka, Hiroyasu; Shiro, Yoshitsugu; Nagano, Shingo

doi:10.1074/jbc.m708109200

Cited by 42 publications

(44 citation statements)

References 25 publications

(37 reference statements)

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“…RseB constitutes a signal transduction pathway leading to the induction of r E expression and is speculated to bind mislocalized lipoproteins to the hydrophobic cavity [20]. VioE is speculated to play a key role in the biosynthesis of violacein [21,22], a purple pigment with antibacterial and cytotoxic properties. Non-specific membrane interaction and discharge of cargos are unfavorable for the functions of these proteins although their exact functions remain to be clarified.…”

Section: Discussionmentioning

confidence: 99%

A short helix in the C‐terminal region of LolA is important for the specific membrane localization of lipoproteins

2008

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The structures of a lipoprotein carrier, LolA, and a lipoprotein receptor, LolB, are similar except for an extra C-terminal loop containing a 3 10 helix and b-strand 12 in LolA. Lipoprotein release was significantly reduced when b-12 was deleted. Deletion of the 3 10 helix also inhibited the lipoprotein release. Furthermore, lipoproteins were non-specifically localized to membranes when LolA lacked the 3 10 helix. Thus, the membrane localization of lipoproteins with the LolA derivative lacking the 3 10 helix was independent of LolB whereas LolB was essential for the outer membrane localization of lipoproteins with the wild-type LolA.

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Section: Discussionmentioning

confidence: 99%

A short helix in the C‐terminal region of LolA is important for the specific membrane localization of lipoproteins

2008

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“…Several proteins in SCOP have somewhat smaller -sheets (11-13 strands) but a similar topology to the DUF1089 sheet (Hirano et al, 2008). Despite the fact that the shapes and curvatures of these sheets vary greatly from an open sheet to a nearly complete barrel, there is growing evidence that many, if not all, could be distantly related.…”

Section: Spiral B-roll: a New Architecture That Might Have Evolved Frmentioning

confidence: 99%

Structural classification of proteins and structural genomics: new insights into protein folding and evolution

Andreeva

2010

Acta Cryst Sect F

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During the past decade, the Protein Structure Initiative (PSI) centres have become major contributors of new families, superfamilies and folds to the Structural Classification of Proteins (SCOP) database. The PSI results have increased the diversity of protein structural space and accelerated our understanding of it. This review article surveys a selection of protein structures determined by the Joint Center for Structural Genomics (JCSG). It presents previously undescribed-sheet architectures such as the double barrel and spiral-roll and discusses new examples of unusual topologies and peculiar structural features observed in proteins characterized by the JCSG and other Structural Genomics centres. structural communications

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“…In the presence of VioE, the reactive IPA imine dimer instead is converted to protodeoxyviolaceinic acid. Structural and biochemical investigations for VioE revealed that the sophisticated [1,2]-indole rearrangement is catalyzed in the absence of any cofactor or metal ion (67).…”

Section: The Atomic Coordinates and Structure Factors (Codes 5g3s 5gmentioning

confidence: 99%

Biosynthesis of Violacein, Structure and Function of l-Tryptophan Oxidase VioA from Chromobacterium violaceum

Füller

Röpke

Krausze

et al. 2016

Journal of Biological Chemistry

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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 ␣-imine catalyzed by the flavoenzyme L-tryptophan oxidase (VioA). A substrate-related (3-(1H-indol-3-yl)-2-methylpropanoic acid) and a product-related (2-(1H-indol-3-ylmethyl)prop-2-enoic acid) competitive VioA inhibitor was synthesized for subsequent kinetic and x-ray crystallographic investigations. Structures of the binary VioA⅐FADH 2 and of the ternary VioA⅐FADH 2 ⅐2-(1H-indol-3-ylmethyl)prop-2-enoic acid complex were resolved. VioA forms a "loosely associated" homodimer as indicated by small-angle x-ray scattering experiments. VioA belongs to the glutathione reductase family 2 of The amino acid tryptophan (Trp) is a versatile metabolite that is shunted into several microbial secondary pathways. The oxidative dimerization of two Trp scaffolds is an essential step for the synthesis of the natural bisindole compounds violacein, rebeccamycin, and staurosporine. The water-insoluble purple pigment violacein is mainly produced by the bacteria Chromobacterium violaceum and Janthinobacterium lividum in tropical habitats where it might be responsible for the shielding against UV radiation (1-3). Various biological activities of violacein, including antibacterial, antiviral, as well as cytotoxic effects against several tumor cell lines, have been demonstrated (4). The related compounds rebeccamycin and staurosporine show strong antitumorigenic activity because of DNA topoisomerase or protein kinase inhibition (5, 6).Synthesis of violacein, rebeccamycin, or staurosporine is based on a closely related initial pathway in which orthologous enzymes catalyze the oxidation of a Trp moiety into the related indole-3-pyruvic acid (IPA) 2 imine by the enzymes VioA, RebO, or StaO ( Fig. 1) (7-9). Subsequently, oxidative coupling of two imines by VioB, RebD, or StaD results in the formation of a short-lived compound that was proposed to be an IPA imine dimer (7, 10). For the synthesis of rebeccamycin and staurosporine, this reactive intermediate is spontaneously converted into chromopyrrolic acid (11-13). By contrast, violacein biosynthesis requires a key intramolecular rearrangement. The postulated IPA imine dimer is the substrate of VioE, which is catalyzing a [1,2]-shift of the indole ring to produce protodeoxyviolaceinic acid (7,14). Fig. 1 gives a schematic overview about the related pathways as follows: common enzymatic reactions and the involved cofactors are highlighted (gray shading), subsequent steps for the synthesis of violacein (VioE, VioD, VioC, and one autocatalytic step) (3, 7), rebeccamycin (RebP, RebC, RebG, and RebM) (15, 16), and staurosporine (StaP, StaC, StaG, StaN, StaMA, and StaMB) (16) are indicated.Synthesis of violacein starts with the FAD-dependent oxidation of L-Trp to IPA imine catalyzed by VioA. The VioA protein from C. violaceum shares a su...

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Crystal Structure of VioE, a Key Player in the Construction of the Molecular Skeleton of Violacein

Cited by 42 publications

References 25 publications

A short helix in the C‐terminal region of LolA is important for the specific membrane localization of lipoproteins

A short helix in the C‐terminal region of LolA is important for the specific membrane localization of lipoproteins

Structural classification of proteins and structural genomics: new insights into protein folding and evolution

Biosynthesis of Violacein, Structure and Function of l-Tryptophan Oxidase VioA from Chromobacterium violaceum

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