ArticleThe EMBO journal2000
The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography.
Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.
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Who cites it
121 citing papers in PubMed, 277 citations in OpenAlex.
- Functional flexibility in bacterial hub proteins is driven by proteome expansion.Scientific reports · 2026Article
- RePol: A high-throughput screen for optimizing membrane protein solubilization and purification using polymers.Protein science : a publication of the Protein Society · 2026Article
- Article
- Protein-Protein Interactions as Promising Molecular Targets for Novel Antimicrobials Aimed at Gram-Negative Bacteria.International journal of molecular sciences · 2025Review
- Cell division protein CdpA organises and anchors the midcell ring in haloarchaea.Nature communications · 2025Article
- High-throughput discovery of inhibitory protein fragments with AlphaFold.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- GpsB interacts with FtsZ in multiple species and may serve as an accessory Z-ring anchor.Molecular biology of the cell · 2025Article
- Mycobacterial FtsZ and inhibitors: a promising target for the anti-tubercular drug development.Molecular diversity · 2024Review
- High-throughput discovery of inhibitory protein fragments with AlphaFold.bioRxiv : the preprint server for biology · 2024Article
- Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024Review
- Proteomics and Its Current Application in Biomedical Area: Concise Review.TheScientificWorldJournal · 2024Review
- AAp-MSMD: Amino Acid Preference Mapping on Protein-Protein Interaction Surfaces Using Mixed-Solvent Molecular Dynamics.Journal of chemical information and modeling · 2023Article
- Anchors: A way for FtsZ filaments to stay membrane bound.Molecular microbiology · 2023Review
- Models versus pathogens: how conserved is the FtsZ in bacteria?Bioscience reports · 2023Review
- The structural integrity of the membrane-embedded bacterial division complex FtsQBL studied with molecular dynamics simulations.Computational and structural biotechnology journal · 2023Article
- Connecting sequence features within the disordered C-terminal linker ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Protealysin Targets the Bacterial Housekeeping Proteins FtsZ and RecA.International journal of molecular sciences · 2022Article
- An enhancer sequence in the intrinsically disordered region of FtsZ promotes polymer-guided substrate processing by ClpXP protease.Protein science : a publication of the Protein Society · 2022Article
- Recruitment of the TolA Protein to Cell Constriction Sites in Escherichia coli via Three Separate Mechanisms, and a Critical Role for FtsWI Activity in Recruitment of both TolA and TolQ.Journal of bacteriology · 2022Article
- Modulators of protein-protein interactions as antimicrobial agents.RSC chemical biology · 2021Review
61 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Escherichia coli, FtsZ, a homologue of eukaryotic tubulins, and ZipA, a membrane-anchored protein that binds to FtsZ, are two essential components of the septal ring structure that mediates cell division. Recent data indicate that ZipA is involved in the assembly of the ring by linking FtsZ to the cytoplasmic membrane and that the ZipA-FtsZ interaction is mediated by their C-terminal domains. We present the X-ray crystal structures of the C-terminal FtsZ-binding domain of ZipA and a complex between this domain and a C-terminal fragment of FtsZ. The ZipA domain is a six-stranded beta-sheet packed against three alpha-helices and contains the split beta-alpha-beta motif found in many RNA-binding proteins. The uncovered side of the sheet incorporates a shallow hydrophobic cavity exposed to solvent. In the complex, the 17-residue FtsZ fragment occupies this entire cavity of ZipA and binds as an extended beta-strand followed by alpha-helix. An alanine-scanning mutagenesis analysis of the FtsZ fragment was also performed, which shows that only a small cluster of the buried FtsZ side chains is critical in binding to ZipA.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.