PDBsum entry: 2r6r

Cell cycle

PDB id: 2r6r

Contents

Protein chain

323 a.a. *

Ligands

GDP

Waters ×282

* Residue conservation analysis

PDB id:

2r6r

Name:

Cell cycle

Title:

Aquifex aeolicus ftsz

Structure:

Cell division protein ftsz. Chain: 1. Engineered: yes

Source:

Aquifex aeolicus. Organism_taxid: 224324. Strain: vf5. Gene: ftsz. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.70Å R-factor: 0.181 R-free: 0.227

Authors:

D.Trambaiolo,M.A.Oliva,J.Lowe

Key ref:

M.A.Oliva et al. (2007). Structural insights into the conformational variability of FtsZ. J Mol Biol, 373, 1229-1242. PubMed id: 17900614 DOI: 10.1016/j.jmb.2007.08.056

Date:

06-Sep-07 Release date: 16-Oct-07

Protein chain

O66809  (FTSZ_AQUAE) -  Cell division protein FtsZ

Seq: 367 a.a.

Struc: 323 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: protein complex (3 terms)
• Biological process: microtubule-based process (6 terms)
• Biochemical function: nucleotide binding (3 terms)

DOI no: 10.1016/j.jmb.2007.08.056

J Mol Biol 373:1229-1242 (2007)

PubMed id: 17900614

Structural insights into the conformational variability of FtsZ.

M.A.Oliva, D.Trambaiolo, J.Löwe.

ABSTRACT

FtsZ is a prokaryotic homologue of the eukaryotic cytoskeletal protein tubulin and plays a central role in prokaryotic cell division. Both FtsZ and tubulin are known to pass through cycles of polymerization and depolymerization, but the structural mechanisms underlying this cycle remain to be determined. Comparison of tubulin structures obtained in different states has led to a model in which the tubulin monomer undergoes a conformational switch between a "straight" form found in the walls of microtubules and a "curved" form associated with depolymerization, and it was proposed recently that this model may apply also to FtsZ. Here, we present new structures of FtsZ from47 Aquifex aeolicus,47 Bacillus subtilis, Methanococcus jannaschii and Pseudomonas aeruginosa that provide strong constraints on any proposed role for a conformational switch in the FtsZ monomer. By comparing the full range of FtsZ structures determined in different crystal forms and nucleotide states, and in the presence or in the absence of regulatory proteins, we find no evidence of a conformational change involving domain movement. Our new structural data make it clear that the previously proposed straight and curved conformations of FtsZ were related to inter-species differences in domain orientation rather than two interconvertible conformations. We propose a new model in which lateral interactions help determine the curvature of protofilaments.

Selected figure(s)

Figure 1.
Figure 1. (a) Ribbon representation of FtsZ structures from M. jannaschii, P. aeruginosa (residues 2–316), A. aeolicus (residues 4–326) and B. subtilis (residues 12–315). The nucleotide-binding domain is coloured dark/light blue, the core helix H7 yellow, and the C-terminal domain red/orange. (b) Protofilament-like structures in crystals of GDP-bound A. aeolicus FtsZ (PDB ID 2RGR) and empty M. jannaschii FtsZ (PDB ID 1W59). The protofilament interface is altered by a sliding movement of the top subunit with respect to the lower subunit in the Aquifex structure (left) and is distorted by a rotation of about 10° in the Methanococcus structure (right).

Figure 5.
Figure 5. The Lattice versus Strain model. The central idea is that lateral interactions can stabilise a strained conformation of the protofilament. The monomer shows no change in conformation related to the nucleotide state. Single protofilaments may prefer to adopt straight or curved conformations, depending on the nucleotide state. Increasing or decreasing the curvature introduces some degree of strain, which may result in distortion of the protofilament interface or the monomer conformation. In higher-order structures formed by lateral association of single protofilaments, the strain of curvature can be offset by the energy of the lateral interactions.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2007, 373, 1229-1242) copyright 2007.

Figures were selected by an automated process.