Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

GTP hydrolysis of cell division protein FtsZ: evidence that the active site is formed by the association of monomers.

Biochemistry - 15 Jan 2002

Scheffers Dirk-Jan, de Wit Janny G, den Blaauwen Tanneke, Driessen Arnold J M

Abstract excerpt

The essential prokaryotic cell division protein FtsZ is a tubulin homologue that forms a ring at the division site. FtsZ forms polymers in a GTP-dependent manner. Recent biochemical evidence has shown that FtsZ forms multimeric structures in vitro and in vivo and functions as a self-activating GTPase. Structural analysis of FtsZ points to an important role for the highly conserved tubulin-like loop 7 (T7-loop) in...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cysteine
Share to Glutamic Acid
Share to GTP Phosphohydrolases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Guanosine Triphosphate

Share to Hydrolysis

Share to Magnesium

Share to Scattering, Radiation

Source

Identifiers

PMID: 11781090
DOI: 10.1021/bi011370i

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

GTP hydrolysis of cell division protein FtsZ: evidence that the active site is formed by the association of monomers.PMID 11781090Read ↗

Structure and Mutational Analyses of Escherichia coli ZapD Reveal Charged Residues Involved in FtsZ Filament Bundling.Semantic proximity Read ↗

Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins.Semantic proximity Read ↗

GTPase activity regulates FtsZ ring positioning in Caulobacter crescentus.Semantic proximity Read ↗

Mapping flexibility and the assembly switch of cell division protein FtsZ by computational and mutational approaches.Semantic proximity Read ↗

Assembly of archaeal cell division protein FtsZ and a GTPase-inactive mutant into double-stranded filaments.Semantic proximity Read ↗

Dimerization or oligomerization of the actin-like FtsA protein enhances the integrity of the cytokinetic Z ring.Semantic proximity Read ↗

Mutations in ftsZ that confer resistance to SulA affect the interaction of FtsZ with GTP.Semantic proximity Read ↗

FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins.Semantic proximity Read ↗

Structure of the Z Ring-associated Protein, ZapD, Bound to the C-terminal Domain of the Tubulin-like Protein, FtsZ, Suggests Mechanism of Z Ring Stabilization through FtsZ Cross-linking.Semantic proximity Read ↗

Bacillus subtilis SepF binds to the C-terminus of FtsZ.Semantic proximity Read ↗

Single tryptophan mutants of FtsZ: nucleotide binding/exchange and conformational transitions.Semantic proximity Read ↗

ftsZ mutations affecting cell division frequency, placement and morphology in Bacillus subtilis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.