Structure of Lumazine Protein, an Optical Transponder of Luminescent Bacteria

Chatwell, Lorenz; Illarionova, Victoria; Illarionov, Boris; Eisenreich, Wolfgang; Huber, Robert; Skerra, Arne; Bacher, Adelbert; Fischer, Markus

doi:10.1016/j.jmb.2008.06.052

Cited by 18 publications

(32 citation statements)

References 37 publications

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“…Both β-barrel domains are composed of six antiparallel β-strands and two or three small α-helices, coinciding well with the structure of riboflavin synthase, for which the same lumazine derivative is a substrate (Fig. 1G) (Liao et al, 2001;Chatwell et al, 2008). The lumazine molecule can only bind to the N-terminal domain of LumP, in a shallow groove comprised of residues of strands β4 and β5 and of helix α2 (Fig.…”

Section: Structure Of Lumazine Proteinsupporting

confidence: 65%

Protein-protein complexation in bioluminescence

et al. 2011

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In this review we summarize the progress made towards understanding the role of protein-protein interactions in the function of various bioluminescence systems of marine organisms, including bacteria, jellyfish and soft corals, with particular focus on methodology used to detect and characterize these interactions. In some bioluminescence systems, protein-protein interactions involve an "accessory protein" whereby a stored substrate is efficiently delivered to the bioluminescent enzyme luciferase. Other types of complexation mediate energy transfer to an "antenna protein" altering the color and quantum yield of a bioluminescence reaction. Spatial structures of the complexes reveal an important role of electrostatic forces in governing the corresponding weak interactions and define the nature of the interaction surfaces. The most reliable structural model is available for the protein-protein complex of the Ca 2+ -regulated photoprotein clytin and green-fluorescent protein (GFP) from the jellyfish Clytia gregaria, solved by means of Xray crystallography, NMR mapping and molecular docking. This provides an example of the potential strategies in studying the transient complexes involved in bioluminescence. It is emphasized that structural studies such as these can provide valuable insight into the detailed mechanism of bioluminescence.

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Section: Structure Of Lumazine Proteinsupporting

confidence: 65%

Protein-protein complexation in bioluminescence

et al. 2011

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“…2A). It was reported that the protein binds to one molecule of lumazine in N-terminal half Chatwell et al, 2008). In this study, to generate a minimal size of fluorescent lumazine protein and to provide a basis for the future binding study, the wild type and the mutant genes for the half of the N-terminal region of lumazine protein from Photobacterium leiognathi, were designed by PCR (Polymerase Chain Reaction) and site directed mutagenesis and expressed to be purified.…”

Section: Fmnh2 + Rcho + O2 → Fmn + H2o + Rcooh + Lightmentioning

confidence: 99%

“…Studies have shown that asparagine 101 and isoleucine 102, located beyond N-terminal region, are involved in binding of the lumazine ligand in additions to the amino acids such as serine 48, threonine 50, and alanine 66 at the binding sites in N-terminal half of lumazine protein Chatwell et al, 2008) (Figs. 2A and 2B).…”

Section: Fmnh2 + Rcho + O2 → Fmn + H2o + Rcooh + Lightmentioning

confidence: 99%

Construction, Expression, and Purification of N-Terminal Variants of Lumazine Protein from Photobacterium leiognathi

Kang¹,

Kim²,

Choi³

et al. 2013

The Korean Journal of Microbiology

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“…18 The lumazine protein has a monomeric structure, which is different from a homotrimer protein of riboflavin synthase. 19,20 It was revealed that the monomeric protein folds into two closely similar domains that are structurally related by pseudo-C2 symmetry, whereby the entire domain topology resembles that of riboflavin synthase. 19 Riboflavin synthase binds to two molecules per protein, whereas lumazine protein bind to one molecule of 6,7-dimethyl-8-ribityllumazine (lumazine).…”

mentioning

confidence: 99%

“…19,20 It was revealed that the monomeric protein folds into two closely similar domains that are structurally related by pseudo-C2 symmetry, whereby the entire domain topology resembles that of riboflavin synthase. 19 Riboflavin synthase binds to two molecules per protein, whereas lumazine protein bind to one molecule of 6,7-dimethyl-8-ribityllumazine (lumazine). 19,20 The lumazine protein has internal amino acid sequence homology between the amino terminal domain (LumP-N) and the carboxy terminal domain (LumP-C) ( Fig.…”

mentioning

confidence: 99%

Spectrofluorometric Properties of N-Terminal Domain of Lumazine Protein from Photobacterium leiognathi

Kang¹,

Kim²,

Lee³

et al. 2013

Bulletin of the Korean Chemical Society

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Lumazine protein is a member of the riboflavin synthase superfamily and the intense fluorescence is caused by non-covalently bound to 6,7-dimethyl 8-ribityllumazine. To figure out the binding modes and the structure of the N-terminal domain of lumazine protein, the wild type of protein extending to amino acid 118 (N-LumP 118 Wt) and mutants of N-LumP 118 V41W, S48W, T50W, D64W, and A66W from Photobacterium leiognathi were purified. The biochemical properties of the wild type and mutants of N-LumP 118 proteins were analyzed by absorbance and fluorescence spectroscope. The peak of absorbance and fluorescence of lumazine ligand were shifted to longer wavelength on binding to N-LumPs. The observed absorbance value at 410 nm of lumazine bound to N-LumP 118 proteins indicate that one mole of N-LumP 118 proteins bind to one mole of ligand of lumazine. Fluorescence analysis show that the maximum peak of fluorescence of N-LumP S48W was shifted to the longest wavelength by binding with 6,7-dimethyl 8-ribityllumazine and was shown to the greatest quench effect by acrylamide among all tryptophan mutants.

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Structure of Lumazine Protein, an Optical Transponder of Luminescent Bacteria

Cited by 18 publications

References 37 publications

Protein-protein complexation in bioluminescence

Protein-protein complexation in bioluminescence

Construction, Expression, and Purification of N-Terminal Variants of Lumazine Protein from Photobacterium leiognathi

Spectrofluorometric Properties of N-Terminal Domain of Lumazine Protein from Photobacterium leiognathi

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