PDBsum entry 1w5e

Cell division

PDB id: 1w5e

Contents

Protein chains

(+ 3 more) 332 a.a. *

Ligands

GTP ×9

Waters ×676

* Residue conservation analysis

PDB id:

1w5e

Name:

Cell division

Title:

Ftsz w319y mutant, p1 (m. Jannaschii)

Structure:

Ftsz. Chain: a, b, c, d, e, f, g, h, i. Engineered: yes. Mutation: yes

Source:

Methanocaldococcus jannaschii. Organism_taxid: 2190. Atcc: 43067. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: c41.

Resolution:

3.00Å R-factor: 0.264 R-free: 0.299

Authors:

M.A.Oliva,S.C.Cordell,J.Lowe

Key ref:

M.A.Oliva et al. (2004). Structural insights into FtsZ protofilament formation. Nat Struct Mol Biol, 11, 1243-1250. PubMed id: 15558053 DOI: 10.1038/nsmb855

Date:

06-Aug-04 Release date: 01-Dec-04

Protein chains

Q57816  (FTSZ1_METJA) -  Cell division protein FtsZ 1 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

Seq: 364 a.a.

Struc: 332 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1038/nsmb855

Nat Struct Mol Biol 11:1243-1250 (2004)

PubMed id: 15558053

Structural insights into FtsZ protofilament formation.

M.A.Oliva, S.C.Cordell, J.Löwe.

ABSTRACT

The prokaryotic tubulin homolog FtsZ polymerizes into a ring structure essential for bacterial cell division. We have used refolded FtsZ to crystallize a tubulin-like protofilament. The N- and C-terminal domains of two consecutive subunits in the filament assemble to form the GTPase site, with the C-terminal domain providing water-polarizing residues. A domain-swapped structure of FtsZ and biochemical data on purified N- and C-terminal domains show that they are independent. This leads to a model of how FtsZ and tubulin polymerization evolved by fusing two domains. In polymerized tubulin, the nucleotide-binding pocket is occluded, which leads to nucleotide exchange being the rate-limiting step and to dynamic instability. In our FtsZ filament structure the nucleotide is exchangeable, explaining why, in this filament, nucleotide hydrolysis is the rate-limiting step during FtsZ polymerization. Furthermore, crystal structures of FtsZ in different nucleotide states reveal notably few differences.

Selected figure(s)

Figure 4.
Figure 4. Detailed view of the intersubunit active sites in MjFtsZ and tubulin. (a) FtsZ dimer. The GTPase domain of the lower subunit is complemented by two aspartates (Asp235 and Asp238) that polarize the attacking water molecule (Wat105). Apart from these residues, which belong to loop T7, S9 and helix H10 of the C-terminal domain of FtsZ are involved in the protofilament contact. (b) / tubulin (PDB entry 1JFF) with -tubulin on top (not the tubulin solution dimer, but the catalytically active contact formed in protofilaments). The general arrangement in the active site is very similar to that of FtsZ with T7, S9 and H10 of the C-terminal (intermediate) domain making the protofilament contact. Very little space would be left for a -phosphate, and the polarizing acidic residue, Glu254, is not in the right position to polarize the attacking water molecule. The tubulin structure was solved at low resolution and exact side chain positions may not be known for all residues.

Figure 5.
Figure 5. A lack of conformational changes in different FtsZ structures. (a) M. jannaschii FtsZ with bound GMPCPP at a resolution of 2.5 Å. GDP-containing crystals were soaked with magnesium and GMCPP in a special buffer to replace the bound nucleotide. The -phosphate occupies the previously identified binding pocket^6, making hydrogen bonding contacts to loop T3. (b) Superposition of M. jannaschii FtsZ active sites: minimal changes are observed between the structures of monomers containing nucleotides and the refolded, empty monomer in completely different space groups and packing arrangements. Stereo drawing.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Mol Biol (2004, 11, 1243-1250) copyright 2004.

Figures were selected by an automated process.