PDBsum entry: 1cwv

Structural protein

PDB id: 1cwv

Contents

Protein chain

484 a.a. *

Ligands

CIT

Waters ×195

* Residue conservation analysis

PDB id:

1cwv

Name:

Structural protein

Title:

Crystal structure of invasin: a bacterial integrin-binding p

Structure:

Invasin. Chain: a. Fragment: c-terminal extracellular fragment. Engineered: yes

Source:

Yersinia pseudotuberculosis. Organism_taxid: 633. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.30Å R-factor: 0.224 R-free: 0.274

Authors:

P.J.Bjorkman,Z.A.Hamburger

Key ref:

Z.A.Hamburger et al. (1999). Crystal structure of invasin: a bacterial integrin-binding protein. Science, 286, 291-295. PubMed id: 10514372 DOI: 10.1126/science.286.5438.291

Date:

26-Aug-99 Release date: 13-Oct-99

Protein chain

P11922  (INVA_YERPS) -  Invasin

Seq: 985 a.a.

Struc: 484 a.a.*

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 

• Cellular component: cell surface (1 term)
• Biological process: pathogenesis (1 term)
• Biochemical function: binding (1 term)

DOI no: 10.1126/science.286.5438.291

Science 286:291-295 (1999)

PubMed id: 10514372

Crystal structure of invasin: a bacterial integrin-binding protein.

Z.A.Hamburger, M.S.Brown, R.R.Isberg, P.J.Bjorkman.

ABSTRACT

The Yersinia pseudotuberculosis invasin protein promotes bacterial entry by binding to host cell integrins with higher affinity than natural substrates such as fibronectin. The 2.3 angstrom crystal structure of the invasin extracellular region reveals five domains that form a 180 angstrom rod with structural similarities to tandem fibronectin type III domains. The integrin-binding surfaces of invasin and fibronectin include similarly located key residues, but in the context of different folds and surface shapes. The structures of invasin and fibronectin provide an example of convergent evolution, in which invasin presents an optimized surface for integrin binding, in comparison with host substrates.

Selected figure(s)

Figure 1.
Fig. 1. (A) Ribbon diagram of the structure of Y. pseudotuberculosis Inv497. Residues implicated in integrin binding [Asp911, Asp811 (7, 20), and possibly Arg883] are green (24). The -helical regions in D5 and a 3[10] helix in D4 are red. The disulfide bond in D5 is yellow, and strands are blue (D4 and D5) or green (D1 through D3). (B) Topology diagrams for domains of invasin and related proteins. Inv497 D5 is shown beside a canonical C-type lectin CRD [from E-selectin (14)]; Inv497 D4 is shown beside a C1-type IgSF domain. The strands are blue, helices are red, and disulfide bonds are yellow. The calcium-binding loop in E-selectin (residues 54 to 89) and its truncated counterpart in Inv497 (residues 956 to 959) are green. (C) (left) Hydrogen bonding pattern of the interrupted helix (18) in D5. Main-chain atoms are shown for residues in the helix (24). Side chains are shown for those residues in which main-chain atoms form hydrogen bonds (dashed light blue lines) across the break in the helix. Other side chains have been omitted for clarity. The carbon- trace of the loop is shown in gray. Red, blue, and black balls are oxygen, nitrogen, and carbon atoms, respectively. (right) The Inv497 model (24) in the region of the loop (gray in left panel) of the interrupted helix superimposed on a 2.3 Å [A]-weighted 2 F[obs] F[calc] annealed omit electron density map contoured at 1.0 (map radius, 3.5 Å) (12). (D) Schematic model of the structure of intact invasin in which the ~500 NH[2]-terminal residues reside in the Yersinia outer membrane (OM) (yellow) in a porin-like structure (7) (red), and the Inv497 portion of invasin (green and blue) projects ~180 Å from the outer membrane.

Figure 2.
Fig. 2. Comparison of interdomain interfaces in integrin-binding regions of Inv497 (D4-D5), fibronectin type III repeats 9 and 10 (D9-D10) (14), and VCAM-1 (D1-D2) (14). Hydrogen bonds are shown as dashed yellow lines. Additional hydrogen bonds, van der Waals contacts, and a three- to fivefold larger interdomain surface area (19) stabilize Inv497 D4-D5 and restrict interdomain flexibility, compared to the other interfaces.

The above figures are reprinted by permission from the AAAs: Science (1999, 286, 291-295) copyright 1999.

Figures were selected by an automated process.