4ALZ

The Yersinia T3SS basal body component YscD reveals a different structural periplasmatic domain organization to known homologue PrgH

Summary for 4ALZ

• Entry DOI: 10.2210/pdb4alz/pdb
• Descriptor: YOP PROTEINS TRANSLOCATION PROTEIN D, PHOSPHATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: membrane protein, t3ss, type 3 secretion, effector transport
• Biological source: YERSINIA ENTEROCOLITICA
• Total number of polymer chains: 1
• Total formula weight: 22741.51

Authors

Schmelz, S.,Wisand, U.,Stenta, M.,Muenich, S.,Widow, U.,Cornelis, G.R.,Heinz, D.W. (deposition date: 2012-03-06, release date: 2013-04-24, Last modification date: 2024-05-08)

Primary citation

Kudryashev, M.,Stenta, M.,Schmelz, S.,Amstutz, M.,Wiesand, U.,Castano-Diez, D.,Degiacomi, M.T.,Munnich, S.,Bleck, C.K.,Kowal, J.,Diepold, A.,Heinz, D.W.,Dal Peraro, M.,Cornelis, G.R.,Stahlberg, H.
In Situ Structural Analysis of the Yersinia Enterocolitica Injectisome.
Elife, 2:00792-, 2013

PubMed Abstract: Injectisomes are multi-protein transmembrane machines allowing pathogenic bacteria to inject effector proteins into eukaryotic host cells, a process called type III secretion. Here we present the first three-dimensional structure of Yersinia enterocolitica and Shigella flexneri injectisomes in situ and the first structural analysis of the Yersinia injectisome. Unexpectedly, basal bodies of injectisomes inside the bacterial cells showed length variations of 20%. The in situ structures of the Y. enterocolitica and S. flexneri injectisomes had similar dimensions and were significantly longer than the isolated structures of related injectisomes. The crystal structure of the inner membrane injectisome component YscD appeared elongated compared to a homologous protein, and molecular dynamics simulations documented its elongation elasticity. The ring-shaped secretin YscC at the outer membrane was stretched by 30-40% in situ, compared to its isolated liposome-embedded conformation. We suggest that elasticity is critical for some two-membrane spanning protein complexes to cope with variations in the intermembrane distance. DOI:http://dx.doi.org/10.7554/eLife.00792.001.

PubMed: 23908767
DOI: 10.7554/ELIFE.00792

Experimental method

X-RAY DIFFRACTION (1.4 Å)