Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD

Schreiner M, Niemann H (2012)
BMC Structural Biology 12(1): 13.

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Abstract / Bemerkung
Background Type III secretion systems are used by Gram-negative bacteria as “macromolecular syringes” to inject effector proteins into eukaryotic cells. Two hydrophobic proteins called translocators form the necessary pore in the host cell membrane. Both translocators depend on binding to a single chaperone in the bacterial cytoplasm to ensure their stability and efficient transport through the secretion needle. It was suggested that the conserved chaperones bind the more divergent translocators via a hexapeptide motif that is found in both translocators and conserved between species. Results We crystallized a synthetic decapeptide from the Yersinia enterocolitica minor type III secretion translocator YopD bound to its cognate chaperone SycD and determined the complex structure at 2.5 Å resolution. The structure of peptide-bound SycD is almost identical to that of apo SycD with an all helical fold consisting of three tetratricopeptide repeats (TPRs) and an additional C-terminal helix. Peptide-bound SycD formed a kinked head-to-head dimer that had previously been observed for the apo form of SycD. The homodimer interface comprises both helices of the first tetratricopeptide repeat. The YopD peptide bound in extended conformation into a mainly hydrophobic groove on the concave side of SycD. TPRs 1 and 2 of SycD form three hydrophobic pockets that accommodated the conserved hydrophobic residues at position 1, 3 and 6 of the translocator hexapeptide sequence. Two tyrosines that are highly conserved among translocator chaperones contribute to the hydrophobic patches but also form hydrogen bonds to the peptide backbone. Conclusions The interaction between SycD and YopD is very similar to the binding of the Pseudomonas minor translocator PopD to its chaperone PcrH and the Shigella major translocator IpaB to its chaperone IpgC. This confirms the prediction made by Kolbe and co-workers that a hexapeptide with hydrophobic residues at three positions is a conserved chaperone binding motif. Because the hydrophobic groove on the concave side of translocator chaperones is involved in binding of the major and the minor translocator, simultaneous binding of both translocators to a single type III secretion class II chaperone appears unlikely.
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BMC Structural Biology
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12
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13
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Article Processing Charge funded by the Deutsche Forschungsgemeinschaft and the Open Access Publication Fund of Bielefeld University.
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Schreiner M, Niemann H. Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD. BMC Structural Biology. 2012;12(1):13.
Schreiner, M., & Niemann, H. (2012). Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD. BMC Structural Biology, 12(1), 13. doi:10.1186/1472-6807-12-13
Schreiner, M., and Niemann, H. (2012). Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD. BMC Structural Biology 12, 13.
Schreiner, M., & Niemann, H., 2012. Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD. BMC Structural Biology, 12(1), p 13.
M. Schreiner and H. Niemann, “Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD”, BMC Structural Biology, vol. 12, 2012, pp. 13.
Schreiner, M., Niemann, H.: Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD. BMC Structural Biology. 12, 13 (2012).
Schreiner, Madeleine, and Niemann, Hartmut. “Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD”. BMC Structural Biology 12.1 (2012): 13.
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2012-09-24T14:21:15Z

9 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

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Solomon R, Zhang W, McCrann G, Bliska JB, Viboud GI., PLoS One 10(3), 2015
PMID: 25807250
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Discola KF, Förster A, Boulay F, Simorre JP, Attree I, Dessen A, Job V., J Biol Chem 289(6), 2014
PMID: 24297169
Binding mode analysis of a major T3SS translocator protein PopB with its chaperone PcrH from Pseudomonas aeruginosa.
Banerjee A, Dey S, Chakraborty A, Datta A, Basu A, Chakrabarti S, Datta S., Proteins 82(12), 2014
PMID: 25116453
The Deinococcus radiodurans DR1245 protein, a DdrB partner homologous to YbjN proteins and reminiscent of type III secretion system chaperones.
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PMID: 23441204
Structure and biophysics of type III secretion in bacteria.
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The SseC translocon component in Salmonella enterica serovar Typhimurium is chaperoned by SscA.
Cooper CA, Mulder DT, Allison SE, Pilar AV, Coombes BK., BMC Microbiol 13(), 2013
PMID: 24090070

60 References

Daten bereitgestellt von Europe PubMed Central.

Yersinia pestis YopD 150-287 fragment is partially unfolded in the native state.
Raab R, Swietnicki W., Protein Expr. Purif. 58(1), 2008
PMID: 18160307
XDS.
Kabsch W., Acta Crystallogr. D Biol. Crystallogr. 66(Pt 2), 2010
PMID: 20124692
Scaling and assessment of data quality.
Evans P., Acta Crystallogr. D Biol. Crystallogr. 62(Pt 1), 2006
PMID: 16369096
The CCP4 suite: programs for protein crystallography.
Collaborative Computational Project, Number 4., Acta Crystallogr. D Biol. Crystallogr. 50(Pt 5), 1994
PMID: 15299374
Phaser crystallographic software.
McCoy AJ, Grosse-Kunstleve RW, Adams PD, Winn MD, Storoni LC, Read RJ., J Appl Crystallogr 40(Pt 4), 2007
PMID: 19461840
Features and development of Coot.
Emsley P, Lohkamp B, Scott WG, Cowtan K., Acta Crystallogr. D Biol. Crystallogr. 66(Pt 4), 2010
PMID: 20383002
MolProbity: all-atom structure validation for macromolecular crystallography.
Chen VB, Arendall WB 3rd, Headd JJ, Keedy DA, Immormino RM, Kapral GJ, Murray LW, Richardson JS, Richardson DC., Acta Crystallogr. D Biol. Crystallogr. 66(Pt 1), 2010
PMID: 20057044

AUTHOR UNKNOWN, 2011
Electrostatics of nanosystems: application to microtubules and the ribosome.
Baker NA, Sept D, Joseph S, Holst MJ, McCammon JA., Proc. Natl. Acad. Sci. U.S.A. 98(18), 2001
PMID: 11517324

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