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  Crystal Structure of PrgI-SipD: Insight into a Secretion Competent State of the Type Three Secretion System Needle Tip and its Interaction with Host Ligands

Lunelli, M., Hurwitz, R., Lambers, J., & Kolbe, M. (2011). Crystal Structure of PrgI-SipD: Insight into a Secretion Competent State of the Type Three Secretion System Needle Tip and its Interaction with Host Ligands. PLoS Pathogens, 7(8): e1002163. doi:10.1371/journal.ppat.1002163.

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Genre: Journal Article
Alternative Title : PLoS Pathog.

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PLoS_Pathogens_2011_7_e1002163.pdf (Publisher version), 656KB
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Lunelli et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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Lunelli, Michele1, Author           
Hurwitz, Robert2, Author           
Lambers, Jutta1, Author           
Kolbe, Michael1, Author           
Affiliations:
1Department of Cellular Microbiology, Max Planck Institute for Infection Biology, Max Planck Society, ou_1664145              
2Core Facilities / Proteinpurification, Max Planck Institute for Infection Biology, Max Planck Society, ou_1664144              

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 Abstract: Many infectious Gram-negative bacteria, including Salmonella typhimurium, require a Type Three Secretion System (T3SS) to translocate virulence factors into host cells. The T3SS consists of a membrane protein complex and an extracellular needle together that form a continuous channel. Regulated secretion of virulence factors requires the presence of SipD at the T3SS needle tip in S. typhimurium. Here we report three-dimensional structures of individual SipD, SipD in fusion with the needle subunit PrgI, and of SipD: PrgI in complex with the bile salt, deoxycholate. Assembly of the complex involves major conformational changes in both SipD and PrgI. This rearrangement is mediated via a p bulge in the central SipD helix and is stabilized by conserved amino acids that may allow for specificity in the assembly and composition of the tip proteins. Five copies each of the needle subunit PrgI and SipD form the T3SS needle tip complex. Using surface plasmon resonance spectroscopy and crystal structure analysis we found that the T3SS needle tip complex binds deoxycholate with micromolar affinity via a cleft formed at the SipD: PrgI interface. In the structure-based three-dimensional model of the T3SS needle tip, the bound deoxycholate faces the host membrane. Recently, binding of SipD with bile salts present in the gut was shown to impede bacterial infection. Binding of bile salts to the SipD: PrgI interface in this particular arrangement may thus inhibit the T3SS function. The structures presented in this study provide insight into the open state of the T3SS needle tip. Our findings present the atomic details of the T3SS arrangement occurring at the pathogen-host interface.

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Language(s): eng - English
 Dates: 2011-08
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: eDoc: 572512
ISI: 000294298100009
DOI: 10.1371/journal.ppat.1002163
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Title: PLoS Pathogens
  Alternative Title : PLoS Pathog.
Source Genre: Journal
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Publ. Info: SAN FRANCISCO : PUBLIC LIBRARY SCIENCE
Pages: - Volume / Issue: 7 (8) Sequence Number: e1002163 Start / End Page: - Identifier: ISSN: 1553-7366