PDBsum entry 1xeu

Cell invasion

PDB id: 1xeu

Contents

Protein chain

263 a.a. *

Waters ×225

* Residue conservation analysis

PDB id:

1xeu

Name:

Cell invasion

Title:

Crystal structure of internalin c from listeria monocytogenes

Structure:

Internalin c. Chain: a. Engineered: yes

Source:

Listeria monocytogenes. Organism_taxid: 1639. Gene: inlc. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.05Å R-factor: 0.202 R-free: 0.243

Authors:

A.Ooi,S.Hussain,A.Seyedarabi,R.W.Pickersgill

Key ref:

A.Ooi et al. (2006). Structure of internalin C from Listeria monocytogenes. Acta Crystallogr D Biol Crystallogr, 62, 1287-1293. PubMed id: 17057330 DOI: 10.1107/S0907444906026746

Date:

13-Sep-04 Release date: 30-Aug-05

Protein chain

P71451  (INLC_LISMG) -  Internalin C from Listeria monocytogenes serotype 1/2a (strain EGD / Mackaness)

Seq: 297 a.a.

Struc: 263 a.a.

DOI no: 10.1107/S0907444906026746

Acta Crystallogr D Biol Crystallogr 62:1287-1293 (2006)

PubMed id: 17057330

Structure of internalin C from Listeria monocytogenes.

A.Ooi, S.Hussain, A.Seyedarabi, R.W.Pickersgill.

ABSTRACT

The crystal structure of internalin C (InlC) from Listeria monocytogenes has been determined at 2.0 A resolution. Several observations implicate InlC in infection: inlC has the same transcriptional activator as other virulence genes, it is only present in pathogenic Listeria strains and an inlC deletion mutant is significantly less virulent. While the extended concave receptor-binding surfaces of the leucine-rich repeat (LRR) domains of internalins A and B have aromatic clusters involved in receptor binding, the corresponding surface of InlC is smaller, flatter and more hydrophilic, suggesting that InlC may be involved in weak or transient associations with receptors; this may help explain why no receptor has yet been discovered for InlC. In contrast, the Ig-like domain, to which the LRR domain is fused, has surface aromatics that may be of functional importance, possibly being involved in binding to the surface of the bacteria or in receptor binding.

Selected figure(s)

Figure 1.
Figure 1 (a) Schematic drawing of the domain structure of internalin C. (b) Electron density around Phe146, one of only two exposed hydrophobic residues on the receptor-binding surface of internalin C; also shown are adjacent leucine residues that contribute to the hydrophobic core of the LRR domain. The 2.0 Å resolution [A]-weighted 2F[obs] - F[calc] map was contoured at 1 . (c) Stereo C^ trace of the internalin C structure. (b) was prepared using BOBSCRIPT (Esnouf, 1997[Esnouf, R. M. (1997). J. Mol. Graph. 15, 132-134.]) and (c) and Fig. 4-(b) were prepared using PyMOL (DeLano, 2002[DeLano, W. L. (2002). The PyMOL Molecular Visualization System. DeLano Scientific, San Carlos, CA, USA. http://www.pymol.org .]).

Figure 2.
Figure 2 (a) Structure of a typical LRR coil of internalin C, comprising 22 residues. The LRR shown is coil four of six present in InlC and corresponds to residues 141-162. The hydrophobic core of the LRR domain is typically formed by leucine residues at positions 2, 5, 7, 12, 15, 18 and 21. There is an asparagine at position 10 in five out of the six turns; the first turn is a variant and the first -strand of the Ig-like domain provides an equivalent glutamine. (b) Structure of the unique 21-residue coil three of InlC (residues 120-140). The 3[10]-helix of the other coils (see a) is missing, replaced by a 1-4 turn (residues 15-18) and a proline at position 19.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2006, 62, 1287-1293) copyright 2006.

Figures were selected by an automated process.