Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2017 Apr 1;73(Pt 4):222-227.
doi: 10.1107/S2053230X17004101. Epub 2017 Mar 22.

Crystal structure of a small heat-shock protein from Xylella fastidiosa reveals a distinct high-order structure

Emanuella Maria Barreto Fonseca  1 , Valéria Scorsato  1 , Marcelo Leite Dos Santos  1 , Atilio Tomazini Júnior  2 , Susely Ferraz Siqueira Tada  3 , Clelton Aparecido Dos Santos  3 , Marcelo Augusto Szymanski de Toledo  3 , Anete Pereira de Souza  3 , Igor Polikarpov  2 , Ricardo Aparicio  1
Affiliations

Crystal structure of a small heat-shock protein from Xylella fastidiosa reveals a distinct high-order structure

Emanuella Maria Barreto Fonseca et al. Acta Crystallogr F Struct Biol Commun. .

Abstract

Citrus variegated chlorosis is a disease that attacks economically important citrus plantations and is caused by the plant-pathogenic bacterium Xylella fastidiosa. In this work, the structure of a small heat-shock protein from X. fastidiosa (XfsHSP17.9) is reported. The high-order structures of small heat-shock proteins from other organisms are arranged in the forms of double-disc, hollow-sphere or spherical assemblies. Unexpectedly, the structure reported here reveals a high-order architecture forming a nearly square cavity.

Keywords: XfsHSP17.9; Xylella fastidiosa; chaperones; citrus variegated chlorosis; small heat-shock protein; α-crystallin domain.

PubMed Disclaimer

Figures

Figure 1
Figure 1
Folding (a) and topology (b) of XfsHSP17.9. The structure consists of seven β-strands and three 310-helices. β-Strands are numbered according to the convention used for M. jannaschii HSP16.5 (Kim et al., 1998 ▸) and X. citri HspA (Hilario et al., 2011 ▸).
Figure 2
Figure 2
(a) Oligomeric structures of other sHSPs for comparison. (b) XfsHSP17.9 dimer–dimer assembly. The enlargement shows the surroundings of Ile145 and Val147. (c) High-order structure of XfsHSP17.9 viewed along the c axis. The formation of nearly square channels is observed along the crystallographic c axis. (d) Hydrogen bonds between the ACD motif and the interdomain loop (the region near helix h2) of the molecule related by crystallographic symmetry. The colours of the ribbons were assigned randomly in order to differentiate between neighbouring protein chains.
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

References

    1. Allen, S. P., Polazzi, J. O., Gierse, J. K. & Easton, A. M. (1992). J. Bacteriol. 174, 6938–6947. - PMC - PubMed
    1. Azzoni, A. R., Tada, S. F. S., Rosselli, L. K., Paula, D. P., Catani, C. F., Sabino, A. A., Barbosa, J. A. R. G., Guimarães, B. G., Eberlin, M. N., Medrano, F. J. & Souza, A. P. (2004). Protein Expr. Purif. 33, 297–303. - PubMed
    1. Bagnéris, C., Bateman, O. A., Naylor, C. E., Cronin, N., Boelens, W. C., Keep, N. H. & Slingsby, C. (2009). J. Mol. Biol. 392, 1242–1252. - PubMed
    1. Beer, T. A. P. de, Berka, K., Thornton, J. M. & Laskowski, R. A. (2014). Nucleic Acids Res. 42, D292–D296. - PMC - PubMed
    1. Bepperling, A., Alte, F., Kriehuber, T., Braun, N., Weinkauf, S., Groll, M., Haslbeck, M. & Buchner, J. (2012). Proc. Natl Acad. Sci. USA, 109, 20407–20412. - PMC - PubMed

MeSH terms