3SZE

Crystal structure of the passenger domain of the E. coli autotransporter EspP

Summary for 3SZE

• Entry DOI: 10.2210/pdb3sze/pdb
• Descriptor: Serine protease espP (2 entities in total)
• Functional Keywords: parallel beta-helix, serine protease, hydrolase
• Biological source: Escherichia coli O157:H7
• Cellular location: Serine protease espP: Periplasm (By similarity). Secreted autotransporter protein espP: Secreted. Autotransporter protein espP translocator: Cell outer membrane; Multi-pass membrane protein (By similarity): Q7BSW5
• Total number of polymer chains: 1
• Total formula weight: 105535.26

Authors

Khan, S.,Mian, H.S.,Sandercock, L.E.,Battaile, K.P.,Lam, R.,Chirgadze, N.Y.,Pai, E.F. (deposition date: 2011-07-18, release date: 2011-10-12, Last modification date: 2024-02-28)

Primary citation

Khan, S.,Mian, H.S.,Sandercock, L.E.,Chirgadze, N.Y.,Pai, E.F.
Crystal Structure of the Passenger Domain of the Escherichia coli Autotransporter EspP.
J.Mol.Biol., 413:985-1000, 2011

PubMed Abstract: Autotransporters represent a large superfamily of known and putative virulence factors produced by Gram-negative bacteria. They consist of an N-terminal "passenger domain" responsible for the specific effector functions of the molecule and a C-terminal "β-domain" responsible for translocation of the passenger across the bacterial outer membrane. Here, we present the 2.5-Å crystal structure of the passenger domain of the extracellular serine protease EspP, produced by the pathogen Escherichia coli O157:H7 and a member of the serine protease autotransporters of Enterobacteriaceae (SPATEs). Like the previously structurally characterized SPATE passenger domains, the EspP passenger domain contains an extended right-handed parallel β-helix preceded by an N-terminal globular domain housing the catalytic function of the protease. Of note, however, is the absence of a second globular domain protruding from this β-helix. We describe the structure of the EspP passenger domain in the context of previous results and provide an alternative hypothesis for the function of the β-helix within SPATEs.

PubMed: 21964244
DOI: 10.1016/j.jmb.2011.09.028

Experimental method

X-RAY DIFFRACTION (2.5 Å)