The Structure of the Oligopeptide-binding Protein, AppA, from Bacillus subtilis in Complex with a Nonapeptide

Levdikov, V.M.; Blagova, E.V.; Brannigan, J.A.; Wright, Lisa; Vagin, A.A.; Wilkinson, Anthony J.

doi:10.1016/j.jmb.2004.10.089

Cited by 69 publications

(89 citation statements)

References 55 publications

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“…The four hydrophobic pockets in PrgZ do not provide much extra space for larger side chains, and they will strongly favor the binding by PrgZ of hydrophobic peptides such as cCF10 and iCF10. Most side chain pockets of AppA from B. subtilis and the nonspecific binding cavity of OppA from L. lactis can more easily adapt to a much greater diversity of amino acids (13,14,32,33). These proteins also have far more hydrophilic side chain pockets than PrgZ (Table 2).…”

Section: Discussionmentioning

confidence: 99%

“…These proteins also have far more hydrophilic side chain pockets than PrgZ (Table 2). Thus, the structural comparison of PrgZ with the homologous chemosensors explains the high selectivity of PrgZ for hydrophobic peptides (cCF10 and iCF10) compared with the promiscuous binding of peptides by the OppA and AppA proteins (14,29,33). It is likely that in E. faecalis, PrgZ and OppA have diverged to obtain different functions to discriminate hydrophobic pheromones from nutritional peptides.…”

Section: Discussionmentioning

confidence: 99%

“…DppA and MppA from E. coli, OppA from S. typhimurium, and AppA from B. subtilis all form salt bridges to both the N and C termini of the bound peptides (29,(33)(34)(35). OppA from L. lactis is an important exception.…”

Section: Discussionmentioning

confidence: 99%

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Structure and Mode of Peptide Binding of Pheromone Receptor PrgZ

Berntsson

Schuurman-Wolters

Dunny

et al. 2012

Journal of Biological Chemistry

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Background: A sex pheromone system controls bacterial conjugation. Results: The initial receptor PrgZ has been crystallized in complex with the sex pheromone cCF10. Conclusion: An extensive network of hydrogen bonds explains the high peptide specificity of PrgZ. Significance: The sex pheromone and inhibitor peptide compete for binding to PrgZ, providing new insight into the regulation of conjugation.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Structure and Mode of Peptide Binding of Pheromone Receptor PrgZ

Berntsson

Schuurman-Wolters

Dunny

et al. 2012

Journal of Biological Chemistry

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“…Of particular interest is the structure of the SBP AppA from Bacillus subtilis (PBD 1XOC, rmsd 1.151 Å for 122 Cα atoms). AppA was copurified and crystallized with a nonapeptide (52). Surface representations of both structures reveal that MbnE is in an open conformation, whereas AppA is in a closed conformation with its nonapeptide substrate inaccessible to solvent (SI Appendix, Fig.…”

Section: Gene Regulation Patterns Of Transport Proteins In Ms Trichomentioning

confidence: 99%

Methanobactin transport machinery

Dassama

Kenney

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Methanotrophic bacteria use methane, a potent greenhouse gas, as their primary source of carbon and energy. The first step in methane metabolism is its oxidation to methanol. In almost all methanotrophs, this chemically challenging reaction is catalyzed by particulate methane monooxygenase (pMMO), a copper-dependent integral membrane enzyme. Methanotrophs acquire copper (Cu) for pMMO by secreting a small ribosomally produced, posttranslationally modified natural product called methanobactin (Mbn). Mbn chelates Cu with high affinity, and the Cu-loaded form (CuMbn) is reinternalized into the cell via an active transport process. Bioinformatic and gene regulation studies suggest that two proteins might play a role in CuMbn handling: the TonB-dependent transporter MbnT and the periplasmic binding protein MbnE. Disruption of the gene that encodes MbnT abolishes CuMbn uptake, as reported previously, and expression of MbnT in Escherichia coli confers the ability to take up CuMbn. Biophysical studies of MbnT and MbnE reveal specific interactions with CuMbn, and a crystal structure of apo MbnE is consistent with MbnE's proposed role as a periplasmic CuMbn transporter. Notably, MbnT and MbnE exhibit different levels of discrimination between cognate and noncognate CuMbns. These findings provide evidence for CuMbn–protein interactions and begin to elucidate the molecular mechanisms of its recognition and transport.

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“…OppAs de Bsu (AppA) complexada com um nonapeptídeo na resolução de 1.55 Å (1xoc) (LEVDIKOV et al, 2005), e Stm (OppA), complexada com um tripeptídeo na resolução de 1.75Å (1jev) (TAME et al, 1996). A estrutura do modelo da OppA de…”

Section: Modelagem Molecular Da Proteína Ligadora De Oligopeptídeos (unclassified

Modelagem molecular das proteínas captadoras de molibdato (ModA) e oligopeptídeos (OppA) de Xanthomonas axonopodis pv. citri .

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The Structure of the Oligopeptide-binding Protein, AppA, from Bacillus subtilis in Complex with a Nonapeptide

Cited by 69 publications

References 55 publications

Structure and Mode of Peptide Binding of Pheromone Receptor PrgZ

Structure and Mode of Peptide Binding of Pheromone Receptor PrgZ

Methanobactin transport machinery

Modelagem molecular das proteínas captadoras de molibdato (ModA) e oligopeptídeos (OppA) de Xanthomonas axonopodis pv. citri .

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