PDBsum entry 1d0b

Cell adhesion

PDB id: 1d0b

Contents

Protein chain

207 a.a. *

Metals

_CA ×2

Waters ×147

* Residue conservation analysis

PDB id:

1d0b

Name:

Cell adhesion

Title:

Internalin b leucine rich repeat domain

Structure:

Internalin b. Chain: a. Fragment: lrr domain, residues 36-248. Engineered: yes

Source:

Listeria monocytogenes. Organism_taxid: 1639. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.86Å R-factor: 0.207 R-free: 0.235

Authors:

M.Marino,L.Braun,P.Cossart,P.Ghosh

Key ref:

M.Marino et al. (1999). Structure of the lnlB leucine-rich repeats, a domain that triggers host cell invasion by the bacterial pathogen L. monocytogenes. Mol Cell, 4, 1063-1072. PubMed id: 10635330 DOI: 10.1016/S1097-2765(00)80234-8

Date:

09-Sep-99 Release date: 07-Jan-00

Protein chain

P0DQD2  (INLB_LISMO) -  Internalin B from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)

Seq: 630 a.a.

Struc: 207 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

DOI no: 10.1016/S1097-2765(00)80234-8

Mol Cell 4:1063-1072 (1999)

PubMed id: 10635330

Structure of the lnlB leucine-rich repeats, a domain that triggers host cell invasion by the bacterial pathogen L. monocytogenes.

M.Marino, L.Braun, P.Cossart, P.Ghosh.

ABSTRACT

The L. monocytogenes protein lnlB activates phosphoinositide 3-kinase and induces phagocytosis in several mammalian cell types. The 1.86 A resolution X-ray crystal structure of the leucine-rich repeat domain of lnlB that is both necessary and sufficient to induce phagocytosis is presented here. The structure supports a crucial role for calcium in host cell invasion by L. monocytogenes and supplies a rationale for its function. Calciums are bound to the protein in an unusually exposed manner that suggests that the metals may act as a bridge between lnlB and mammalian cell surface receptors. The structure also identifies surfaces on the curved and elongated molecule that may constitute additional interaction sites in forming a bacterial-mammalian signaling complex.

Selected figure(s)

Figure 1.
Figure 1. InlB LRR Domainα and 3[10] helices are in cyan, β strands are in red, and loops are in green. The domain consists of the N-terminal cap region (residues 36–76) and the LRR region (residues 77–242). Calciums are depicted as blue spheres. This and remaining figures were generated with MOLSCRIPT ([32]) and Raster3D ( [41]).

Figure 5.
Figure 5. Leucine-Rich Repeats(A) Structure of a single 22-residue InlB LRR. Backbone carbons are gray; side chain carbons of conserved or restricted residues are orange; nitrogens and oxygens are blue and red, respectively. Hydrogen bonds are shown as black dotted lines. The location of the β strand and 3[10]-helix are shown for reference. Repeat positions 7 to 10 form a distorted type II (β[P]γ) turn, and repeat positions 21 to 2 (of the following repeat) form a type I (αα) turn.(B) Alignment of the seven and one-half LRRs of InlB (residues 77–242). The consensus repeat sequence is shown below and contains the most commonly occurring residue; the “s” at position 17 denotes a small residue.

The above figures are reprinted by permission from Cell Press: Mol Cell (1999, 4, 1063-1072) copyright 1999.

Figures were selected by the author.