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Article

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

Journal of bacteriology - 1 Jun 2016

Roach Elyse J, Wroblewski Charles, Seidel Laura, Berezuk Alison M, Brewer Dyanne, Kimber Matthew S, Khursigara Cezar M

Abstract excerpt

UNLABELLED: Bacterial cell division is an essential and highly coordinated process. It requires the polymerization of the tubulin homologue FtsZ to form a dynamic ring (Z-ring) at midcell. Z-ring formation relies on a group of FtsZ-associated proteins (Zap) for stability throughout the process of division. In Escherichia coli, there are currently five Zap proteins (ZapA through ZapE), of which four (ZapA, ZapB,...

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PMID: 27021560
DOI: 10.1128/JB.00969-15
PMCID: PMC4959286

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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