1rlu

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models 1rlu, resolution 2.08Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Mycobacterium tuberculosis FtsZ in complex with GTP-gamma-S

Overview

We report three crystal structures of the Mycobacterium tuberculosis cell, division protein FtsZ, as the citrate, GDP, and GTPgammaS complexes, determined at 1.89, 2.60, and 2.08A resolution. MtbFtsZ crystallized as a, tight, laterally oriented dimer distinct from the longitudinal polymer, observed for alphabeta-tubulin. Mutational data on Escherichia coli FtsZ, suggest that this dimer interface is important for proper protofilament, and "Z-ring" assembly and function. An alpha-to-beta secondary structure, conformational switch at the dimer interface is spatially analogous to, and has many of the hallmarks of, the Switch I conformational changes, exhibited by G-proteins upon activation. The presence of a gamma-phosphate, in the FtsZ active site modulates the conformation of the "tubulin" loop, T3 (spatially analogous to the G-protein Switch II); T3 switching upon, gamma-phosphate ligation is directly coupled to the alpha-to-beta switch, by steric overlap. The dual conformational switches observed here for the, first time in an FtsZ link GTP binding and hydrolysis to FtsZ (and, tubulin) lateral assembly and Z-ring contraction, and they are suggestive, of an underappreciated functional analogy between FtsZ, tubulin and, G-proteins.

About this Structure

1RLU is a Single protein structure of sequence from Mycobacterium tuberculosis with GSP and GOL as ligands. Full crystallographic information is available from OCA.

Reference

Structure of Mycobacterium tuberculosis FtsZ reveals unexpected, G protein-like conformational switches., Leung AK, Lucile White E, Ross LJ, Reynolds RC, DeVito JA, Borhani DW, J Mol Biol. 2004 Sep 17;342(3):953-70. PMID:15342249

Page seeded by OCA on Wed Nov 21 01:41:59 2007