PDBsum entry: 1ofu

Bacterial cell division inhibitor

PDB id: 1ofu

Contents

Protein chains

307 a.a. *

119 a.a. *

Ligands

GDP ×2

Waters ×441

* Residue conservation analysis

PDB id:

1ofu

Name:

Bacterial cell division inhibitor

Title:

Crystal structure of sula:ftsz from pseudomonas aeruginosa

Structure:

Hypothetical protein pa3008. Chain: x, y. Fragment: residues 43-161. Synonym: sula. Engineered: yes. Other_details: first 42 residues removed from n-terminus. Cell division protein ftsz. Chain: a, b. Fragment: residues 1-320.

Source:

Pseudomonas aeruginosa. Organism_taxid: 287. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Tetramer (from PDB file)

Resolution:

2.10Å R-factor: 0.215 R-free: 0.255

Authors:

S.C.Cordell,E.J.H.Robinson,J.Lowe

Key ref:

S.C.Cordell et al. (2003). Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ. Proc Natl Acad Sci U S A, 100, 7889-7894. PubMed id: 12808143 DOI: 10.1073/pnas.1330742100

Date:

21-Apr-03 Release date: 19-Jun-03

Protein chains

P47204  (FTSZ_PSEAE) -  Cell division protein FtsZ

Seq: 394 a.a.

Struc: 307 a.a.

Protein chains

Q9HZJ8  (SULA_PSEAE) -  Cell division inhibitor SulA

Seq: 161 a.a.

Struc: 119 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: protein complex (3 terms)
• Biological process: negative regulation of cell division (3 terms)
• Biochemical function: GTP binding (2 terms)

DOI no: 10.1073/pnas.1330742100

Proc Natl Acad Sci U S A 100:7889-7894 (2003)

PubMed id: 12808143

Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ.

S.C.Cordell, E.J.Robinson, J.Lowe.

ABSTRACT

SulA halts cell division in Escherichia coli by binding to the major component of the division machinery FtsZ. We have solved the crystal structure of SulA alone and in complex with FtsZ from Pseudomonas aeruginosa. SulA is expressed when the SOS response is induced. This is a mechanism to inhibit cell division and repair DNA in the event of DNA damage. FtsZ is a tubulin-like protein that forms polymers, with the active-site GTPase split across two monomers. One monomer provides the GTP-binding site and the other, through its T7 loop nucleotide hydrolysis. Our structures show that SulA is a dimer, and that SulA inhibits cell division neither by binding the nucleotide-binding site nor by inducing conformational changes in FtsZ. Instead, SulA binds the T7 loop surface of FtsZ, opposite the nucleotide-binding site, blocking polymer formation. These findings explain why GTP hydrolysis and polymer turnover are required for SulA inhibition.

Selected figure(s)

Figure 3.
Fig. 3. Structural similarity of the SulA monomer (PDB ID code 1OFT) and the N-terminal domain of E. coli RecA (PDB ID code 2REB [PDB] ; ref. 33). The structures have been aligned with an rms deviation of 2.4 Å over 112 C atoms (of 119 for SulA).

Figure 6.
Fig. 6. Model showing how SulA could crosslink the ends of FtsZ protofilaments. The complex is as in Fig. 4. FtsZ monomers, shown in gray, could theoretically bind to each and of the complex in a protofilament-like structure where the T7 loop from one monomer contacts the GTP-binding site from the previous monomer (17).

Figures were selected by the author.