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5KE1

Structure of a C-terminal fragment of the IcsA/VirG passenger-domain

Summary for 5KE1
Entry DOI10.2210/pdb5ke1/pdb
DescriptorOuter membrane protein IcsA autotransporter, NICKEL (II) ION (3 entities in total)
Functional Keywordsvirulence factor, autochaperone, autotransporter, transport protein
Biological sourceShigella flexneri
Cellular locationOuter membrane protein IcsA autotransporter: Periplasm. Outer membrane protein IcsA: Secreted. Outer membrane protein IcsA translocator: Cell outer membrane ; Multi-pass membrane protein : Q7BCK4
Total number of polymer chains2
Total formula weight73261.85
Authors
Leupold, S.,Scrima, A. (deposition date: 2016-06-09, release date: 2017-03-15, Last modification date: 2024-01-10)
Primary citationLeupold, S.,Busing, P.,Mas, P.J.,Hart, D.J.,Scrima, A.
Structural insights into the architecture of the Shigella flexneri virulence factor IcsA/VirG and motifs involved in polar distribution and secretion.
J. Struct. Biol., 198:19-27, 2017
Cited by
PubMed Abstract: IcsA/VirG is a key virulence factor of the human pathogen Shigella flexneri, acting as both an adhesin and actin-polymerizing factor during infection. We identified a soluble expression construct of the IcsA/VirG α-domain using the ESPRIT library screening system and determined its structure to 1.9Å resolution. In addition to the previously characterized autochaperone domain, our structure reveals a new domain, which shares a common fold with the autochaperone domains of various autotransporters. We further provide insight into the previously structurally uncharacterized β-helix domain that harbors the polar targeting motif and passenger-associated transport repeat. This structure is the first of any member of the recently identified passenger-associated transport repeat-containing autotransporters. Thus, it provides new insights into the overall architecture of this class of autotransporters, the function of the identified additional autochaperone domain and the structural properties of motifs involved in polar targeting and secretion of the Shigella flexneri virulence factor IcsA/VirG.
PubMed: 28268178
DOI: 10.1016/j.jsb.2017.03.003
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

227344

數據於2024-11-13公開中

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