1F46

THE BACTERIAL CELL-DIVISION PROTEIN ZIPA AND ITS INTERACTION WITH AN FTSZ FRAGMENT REVEALED BY X-RAY CRYSTALLOGRAPHY

1F46 の概要

• エントリーDOI: 10.2210/pdb1f46/pdb
• 分子名称: CELL DIVISION PROTEIN ZIPA (2 entities in total)
• 機能のキーワード: cell division protein zipa, cell division, transmembrane, inner membrane, cell cycle
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Single-pass type I membrane protein: P77173
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31323.81

構造登録者

Mosyak, L.,Zhang, Y.,Glasfeld, E.,Stahl, M.,Somers, W.S. (登録日: 2000-06-07, 公開日: 2001-06-13, 最終更新日: 2024-02-07)

主引用文献

Mosyak, L.,Zhang, Y.,Glasfeld, E.,Haney, S.,Stahl, M.,Seehra, J.,Somers, W.S.
The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography.
EMBO J., 19:3179-3191, 2000

PubMed 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.

PubMed: 10880432
DOI: 10.1093/emboj/19.13.3179

実験手法

X-RAY DIFFRACTION (1.5 Å)