Structure of Rhodococcus equi virulence-associated protein B (VapB) reveals an eight-stranded antiparallel β-barrel consisting of two Greek-key motifs

Geerds C, Wohlmann J, Haas A, Niemann H (2014)
Acta crystallographica. Section F, Structural biology communications 70(Pt 7): 866-871.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Autor*in
Geerds, ChristinaUniBi; Wohlmann, Jens; Haas, Albert; Niemann, HartmutUniBi
Abstract / Bemerkung
Members of the virulence-associated protein (Vap) family from the pathogen Rhodococcus equi regulate virulence in an unknown manner. They do not share recognizable sequence homology with any protein of known structure. VapB and VapA are normally associated with isolates from pigs and horses, respectively. To contribute to a molecular understanding of Vap function, the crystal structure of a protease-resistant VapB fragment was determined at 1.4 Å resolution. The structure was solved by SAD phasing employing the anomalous signal of one endogenous S atom and two bound Co ions with low occupancy. VapB is an eight-stranded antiparallel β-barrel with a single helix. Structural similarity to avidins suggests a potential binding function. Unlike other eight- or ten-stranded β-barrels found in avidins, bacterial outer membrane proteins, fatty-acid-binding proteins and lysozyme inhibitors, Vaps do not have a next-neighbour arrangement but consist of two Greek-key motifs with strand order 41238567, suggesting an unusual or even unique topology.
Erscheinungsjahr
2014
Zeitschriftentitel
Acta crystallographica. Section F, Structural biology communications
Band
70
Ausgabe
Pt 7
Seite(n)
866-871
ISSN
2053-230X
eISSN
2053-230X
Page URI
https://pub.uni-bielefeld.de/record/2685751

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Geerds C, Wohlmann J, Haas A, Niemann H. Structure of Rhodococcus equi virulence-associated protein B (VapB) reveals an eight-stranded antiparallel β-barrel consisting of two Greek-key motifs. Acta crystallographica. Section F, Structural biology communications. 2014;70(Pt 7):866-871.
Geerds, C., Wohlmann, J., Haas, A., & Niemann, H. (2014). Structure of Rhodococcus equi virulence-associated protein B (VapB) reveals an eight-stranded antiparallel β-barrel consisting of two Greek-key motifs. Acta crystallographica. Section F, Structural biology communications, 70(Pt 7), 866-871. doi:10.1107/S2053230X14009911
Geerds, Christina, Wohlmann, Jens, Haas, Albert, and Niemann, Hartmut. 2014. “Structure of Rhodococcus equi virulence-associated protein B (VapB) reveals an eight-stranded antiparallel β-barrel consisting of two Greek-key motifs”. Acta crystallographica. Section F, Structural biology communications 70 (Pt 7): 866-871.
Geerds, C., Wohlmann, J., Haas, A., and Niemann, H. (2014). Structure of Rhodococcus equi virulence-associated protein B (VapB) reveals an eight-stranded antiparallel β-barrel consisting of two Greek-key motifs. Acta crystallographica. Section F, Structural biology communications 70, 866-871.
Geerds, C., et al., 2014. Structure of Rhodococcus equi virulence-associated protein B (VapB) reveals an eight-stranded antiparallel β-barrel consisting of two Greek-key motifs. Acta crystallographica. Section F, Structural biology communications, 70(Pt 7), p 866-871.
C. Geerds, et al., “Structure of Rhodococcus equi virulence-associated protein B (VapB) reveals an eight-stranded antiparallel β-barrel consisting of two Greek-key motifs”, Acta crystallographica. Section F, Structural biology communications, vol. 70, 2014, pp. 866-871.
Geerds, C., Wohlmann, J., Haas, A., Niemann, H.: Structure of Rhodococcus equi virulence-associated protein B (VapB) reveals an eight-stranded antiparallel β-barrel consisting of two Greek-key motifs. Acta crystallographica. Section F, Structural biology communications. 70, 866-871 (2014).
Geerds, Christina, Wohlmann, Jens, Haas, Albert, and Niemann, Hartmut. “Structure of Rhodococcus equi virulence-associated protein B (VapB) reveals an eight-stranded antiparallel β-barrel consisting of two Greek-key motifs”. Acta crystallographica. Section F, Structural biology communications 70.Pt 7 (2014): 866-871.

5 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

VapA of Rhodococcus equi binds phosphatidic acid.
Wright LM, Carpinone EM, Bennett TL, Hondalus MK, Starai VJ., Mol Microbiol 107(3), 2018
PMID: 29205554
Resonance assignments of a VapC family toxin from Clostridium thermocellum.
Wang C, Xuan J, Cui Q, Feng Y., Biomol NMR Assign 10(2), 2016
PMID: 27386855
Structural characterisation of the virulence-associated protein VapG from the horse pathogen Rhodococcus equi.
Okoko T, Blagova EV, Whittingham JL, Dover LG, Wilkinson AJ., Vet Microbiol 179(1-2), 2015
PMID: 25746683
Transcriptome reprogramming by plasmid-encoded transcriptional regulators is required for host niche adaption of a macrophage pathogen.
Coulson GB, Miranda-CasoLuengo AA, Miranda-CasoLuengo R, Wang X, Oliver J, Willingham-Lane JM, Meijer WG, Hondalus MK., Infect Immun 83(8), 2015
PMID: 26015480

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