Structure of a three-dimensional domain-swapped dimer of the Helicobacter pylori type IV secretion system pilus protein CagL

Barden S, Schomburg B, Conradi J, Backert S, Sewald N, Niemann H (2014)
Acta crystallographica. Section D, Biological crystallography 70(Pt 5): 1391-1400.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Abstract / Bemerkung
A new crystal form of the Helicobacter pylori type IV secretion system (T4SS) pilus protein CagL is described here. In contrast to two previously reported monomeric structures, CagL forms a three-dimensional domain-swapped dimer. CagL dimers can arise during refolding from inclusion bodies or can form spontaneously from purified monomeric CagL in the crystallization conditions. Monomeric CagL forms a three-helix bundle, with which the N-terminal helix is only loosely associated. In the new crystal form, the N-terminal helix is missing. The domain swap is owing to exchange of the C-terminal helix between the two protomers of a dimer. A loop-to-helix transition results in a long helix of 108 amino acids comprising the penultimate and the last helix of the monomer. The RGD motif of dimeric CagL adopts an α-helical conformation. In contrast to the previously reported structures, the conserved and functionally important C-terminal hexapeptide is resolved. It extends beyond the three-helix bundle as an exposed helical appendage. This new crystal form contributes to the molecular understanding of CagL by highlighting rigid and flexible regions in the protein and by providing the first view of the C-terminus. Based on the structural features, a previously unrecognized homology between CagL and CagI is discussed.
Erscheinungsjahr
2014
Zeitschriftentitel
Acta crystallographica. Section D, Biological crystallography
Band
70
Ausgabe
Pt 5
Seite(n)
1391-1400
ISSN
1399-0047
eISSN
1399-0047
Page URI
https://pub.uni-bielefeld.de/record/2676579

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Barden S, Schomburg B, Conradi J, Backert S, Sewald N, Niemann H. Structure of a three-dimensional domain-swapped dimer of the Helicobacter pylori type IV secretion system pilus protein CagL. Acta crystallographica. Section D, Biological crystallography. 2014;70(Pt 5):1391-1400.
Barden, S., Schomburg, B., Conradi, J., Backert, S., Sewald, N., & Niemann, H. (2014). Structure of a three-dimensional domain-swapped dimer of the Helicobacter pylori type IV secretion system pilus protein CagL. Acta crystallographica. Section D, Biological crystallography, 70(Pt 5), 1391-1400. doi:10.1107/S1399004714003150
Barden, S., Schomburg, B., Conradi, J., Backert, S., Sewald, N., and Niemann, H. (2014). Structure of a three-dimensional domain-swapped dimer of the Helicobacter pylori type IV secretion system pilus protein CagL. Acta crystallographica. Section D, Biological crystallography 70, 1391-1400.
Barden, S., et al., 2014. Structure of a three-dimensional domain-swapped dimer of the Helicobacter pylori type IV secretion system pilus protein CagL. Acta crystallographica. Section D, Biological crystallography, 70(Pt 5), p 1391-1400.
S. Barden, et al., “Structure of a three-dimensional domain-swapped dimer of the Helicobacter pylori type IV secretion system pilus protein CagL”, Acta crystallographica. Section D, Biological crystallography, vol. 70, 2014, pp. 1391-1400.
Barden, S., Schomburg, B., Conradi, J., Backert, S., Sewald, N., Niemann, H.: Structure of a three-dimensional domain-swapped dimer of the Helicobacter pylori type IV secretion system pilus protein CagL. Acta crystallographica. Section D, Biological crystallography. 70, 1391-1400 (2014).
Barden, Stephan, Schomburg, Benjamin, Conradi, Jens, Backert, Steffen, Sewald, Norbert, and Niemann, Hartmut. “Structure of a three-dimensional domain-swapped dimer of the Helicobacter pylori type IV secretion system pilus protein CagL”. Acta crystallographica. Section D, Biological crystallography 70.Pt 5 (2014): 1391-1400.

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