3bz5

From Proteopedia

proteopedia linkproteopedia link

Template:STRUCTURE 3bz5

Functional domain of InlJ from Listeria monocytogenes includes a cysteine ladder

Overview

We report on the crystal structure of the internalin domain of InlJ, a virulence-associated surface protein of Listeria monocytogenes, at 2.7-A resolution. InlJ is a member of the internalin family of listerial cell surface proteins characterized by a common N-terminal domain. InlJ bears 15 leucine-rich repeats (LRRs), the same number as in InlA, the prototypical internalin family member. The LRRs of InlJ differ from those of other internalins by having 21, rather than 22, residues and by replacing 1 LRR-defining hydrophobic residue with a conserved cysteine. These cysteines stack to form an intramolecular ladder and regular hydrophobic interactions in consecutive repeats. Analyzing the curvature, twist, and lateral bending angles of InlJ and comparing these with several other LRR proteins, we provide a systematic geometric comparison of LRR protein structures (http://bragi2.helmholtz-hzi.de/Angulator/). These indicate that both cysteine and asparagine ladders stabilize the LRR fold, whereas substitutions in some repeat positions are more likely than others to induce changes in LRR geometry.

About this Structure

3BZ5 is a Single protein structure of sequence from Listeria monocytogenes. Full crystallographic information is available from OCA.

Reference

Crystal structure and standardized geometric analysis of InlJ, a listerial virulence factor and leucine-rich repeat protein with a novel cysteine ladder., Bublitz M, Holland C, Sabet C, Reichelt J, Cossart P, Heinz DW, Bierne H, Schubert WD, J Mol Biol. 2008 Apr 18;378(1):87-96. Epub 2008 Feb 20. PMID:18343406 Page seeded by OCA on Wed Jun 18 12:08:30 2008