ISDA: 1Q5Z

Deposition Date 2003-08-11

Release Date 2003-10-07

Last Version Date 2024-02-14

Entry Detail

PDB ID:

1Q5Z

Keywords:

CELL INVASION

Title:

Crystal Structure of the C-terminal Actin Binding Domain of Salmonella Invasion Protein A (SipA)

Biological Source:

Source Organism(s):

Salmonella typhimurium (Taxon ID: 602)

Expression System(s):

Escherichia coli bl21(de3)

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

1.80 Å

R-Value Free:

0.22

R-Value Work:

0.19

R-Value Observed:

0.19

Space Group:

P 43 21 2

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Macromolecular Entities

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:SipA
Chain IDs:A
Chain Length:177
Number of Molecules:1
Biological Source:Salmonella typhimurium

UniProt ID:P0CL52 Pfam ID:PF22163

Primary Citation

Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms.

Lilic, M, Galkin, V.E, Orlova, A, VanLoock, M.S, Egelman, E.H, Stebbins, C.E.Show

Science 301 1918 1921 (2003)

PMID: 14512630 DOI: 10.1126/science.1088433

Abstact

Like many bacterial pathogens, Salmonella spp. use a type III secretion system to inject virulence proteins into host cells. The Salmonella invasion protein A (SipA) binds host actin, enhances its polymerization near adherent extracellular bacteria, and contributes to cytoskeletal rearrangements that internalize the pathogen. By combining x-ray crystallography of SipA with electron microscopy and image analysis of SipA-actin filaments, we show that SipA functions as a "molecular staple," in which a globular domain and two nonglobular "arms" mechanically stabilize the filament by tethering actin subunits in opposing strands. Deletion analysis of the tethering arms provides strong support for this model.

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Primary Citation of related structures

Abstact

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