PDBsum entry 3vpa

Cell cycle

PDB id: 3vpa

Contents

Protein chains

289 a.a.

Waters ×139

PDB id:

3vpa

Name:

Cell cycle

Title:

Staphylococcus aureus ftsz apo-form

Structure:

Cell division protein ftsz. Chain: a, b, c, d. Fragment: unp residues 12-316. Engineered: yes

Source:

Staphylococcus aureus. Organism_taxid: 158878. Strain: mu50. Gene: ftsz. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.49Å R-factor: 0.212 R-free: 0.258

Authors:

T.Matsui,J.Yamane,N.Mogi,M.Yao,I.Tanaka

Key ref:

T.Matsui et al. (2012). Structural reorganization of the bacterial cell-division protein FtsZ from Staphylococcus aureus. Acta Crystallogr D Biol Crystallogr, 68, 1175-1188. PubMed id: 22948918

Date:

28-Feb-12 Release date: 29-Aug-12

Protein chains

P0A029  (FTSZ_STAAM) -  Cell division protein FtsZ from Staphylococcus aureus (strain Mu50 / ATCC 700699)

Seq: 390 a.a.

Struc: 289 a.a.

Acta Crystallogr D Biol Crystallogr 68:1175-1188 (2012)

PubMed id: 22948918

Structural reorganization of the bacterial cell-division protein FtsZ from Staphylococcus aureus.

T.Matsui, J.Yamane, N.Mogi, H.Yamaguchi, H.Takemoto, M.Yao, I.Tanaka.

ABSTRACT

FtsZ is a key molecule in bacterial cell division. In the presence of GTP, it polymerizes into tubulin-like protofilaments by head-to-tail association. Protofilaments of FtsZ seem to adopt a straight or a curved conformation in relation to the bound nucleotide. However, although several bacterial and archaeal FtsZ structures have been determined, all of the structures reported previously are considered to have a curved conformation. In this study, structures of FtsZ from Staphylococcus aureus (SaFtsZ) were determined in apo, GDP-bound and inhibitor-complex forms and it was found that SaFtsZ undergoes marked conformational changes. The accumulated evidence suggests that the GDP-bound structure has the features of the straight form. The structural change between the curved and straight forms shows intriguing similarity to the eukaryotic cytoskeletal protein tubulin. Furthermore, the structure of the apo form showed an unexpectedly large conformational change in the core region. FtsZ has also been recognized as a novel target for antibacterial drugs. The structure of the complex with the inhibitor PC190723, which has potent and selective antistaphylococcal activity, indicated that the inhibitor binds at the cleft between the two subdomains.