1UTA

Solution structure of the C-terminal RNP domain from the divisome protein FtsN

1UTA の概要

• エントリーDOI: 10.2210/pdb1uta/pdb
• 分子名称: CELL DIVISION PROTEIN FTSN (1 entity in total)
• 機能のキーワード: bacterial cell division protein, rnp domain, cell division, transmembrane, inner membrane
• 由来する生物種: ESCHERICHIA COLI
• 細胞内の位置: Cell inner membrane ; Single-pass type II membrane protein : P29131
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8928.04

構造登録者

Yang, J.-C.,van den Ent, F.,Neuhaus, D.,Brevier, J.,Lowe, J. (登録日: 2003-12-04, 公開日: 2004-09-24, 最終更新日: 2024-05-15)

主引用文献

Yang, J.-C.,van den Ent, F.,Neuhaus, D.,Brevier, J.,Lowe, J.
Solution Structure and Domain Architecture of the Divisome Protein Ftsn
Mol.Microbiol., 52:651-, 2004

PubMed Abstract: Prokaryotic cell division occurs through the formation of a septum, which in Escherichia coli requires coordination of the invagination of the inner membrane, biosynthesis of peptidoglycan and constriction of the outer membrane. FtsN is an essential cell division protein and forms part of the divisome, a putative complex of proteins located in the cytoplasmic membrane. Structural analyses of FtsN by nuclear magnetic resonance (NMR) reveals an RNP-like fold at the C-terminus (comprising residues 243-319), which has significant sequence homology to a peptidoglycan-binding domain. Sequential deletion mutagenesis in combination with NMR shows that the remaining of the periplasmic region of FtsN is unfolded, with the exception of three short, only partially formed helices following the trans-membrane helix. Based on these findings we propose a model in which FtsN, anchored in the inner membrane, bridges over to the peptidoglycan layer, thereby enabling the coordination of the divisome and the murein-shaping machinery in the periplasm.

PubMed: 15101973
DOI: 10.1111/J.1365-2958.2004.03991.X

実験手法

SOLUTION NMR