PDBsum entry 4u09

Unknown function

PDB id: 4u09

Contents

Protein chains

392 a.a.

Ligands

MES ×3

SO4

PEG

Metals

_CL ×4

_ZN ×6

Waters ×609

PDB id:

4u09

Name:

Unknown function

Title:

Structure of leptospira interrogans lrr protein lic12759

Structure:

Lic12759. Chain: a, b. Synonym: lic12759. Engineered: yes

Source:

Leptospira interrogans serovar copenhageni str. Fiocruz l1-130. Organism_taxid: 267671. Gene: lic_12759. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: plyss.

Resolution:

1.95Å R-factor: 0.187 R-free: 0.213

Authors:

W.Shepard,F.A.Saul,A.Haouz,M.Picardeau

Key ref:

I.Miras et al. (2015). Structural characterization of a novel subfamily of leucine-rich repeat proteins from the human pathogen Leptospira interrogans. Acta Crystallogr D Biol Crystallogr, 71, 1351-1359. PubMed id: 26057675 DOI: 10.1107/S139900471500704X

Date:

11-Jul-14 Release date: 03-Jun-15

Protein chains

Q72NS0  (Q72NS0_LEPIC) -  Cytoplasmic membrane protein from Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)

Seq: 423 a.a.

Struc: 392 a.a.

DOI no: 10.1107/S139900471500704X

Acta Crystallogr D Biol Crystallogr 71:1351-1359 (2015)

PubMed id: 26057675

Structural characterization of a novel subfamily of leucine-rich repeat proteins from the human pathogen Leptospira interrogans.

I.Miras, F.Saul, M.Nowakowski, P.Weber, A.Haouz, W.Shepard, M.Picardeau.

ABSTRACT

Pathogenic Leptospira spp. are the agents of leptospirosis, an emerging zoonotic disease. Analyses of Leptospira genomes have shown that the pathogenic leptospires (but not the saprophytes) possess a large number of genes encoding proteins containing leucine-rich repeat (LRR) domains. In other pathogenic bacteria, proteins with LRR domains have been shown to be involved in mediating host-cell attachment and invasion, but their functions remain unknown in Leptospira. To gain insight into the potential function of leptospiral LRR proteins, the crystal structures of four LRR proteins that represent a novel subfamily with consecutive stretches of a 23-amino-acid LRR repeat motif have been solved. The four proteins analyzed adopt the characteristic α/β-solenoid horseshoe fold. The exposed residues of the inner concave surfaces of the solenoid, which constitute a putative functional binding site, are not conserved. The various leptospiral LRR proteins could therefore recognize distinct structural motifs of different host proteins and thus serve separate and complementary functions in the physiology of these bacteria.