1UTA

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

Summary for 1UTA

• Entry DOI: 10.2210/pdb1uta/pdb
• Descriptor: CELL DIVISION PROTEIN FTSN (1 entity in total)
• Functional Keywords: bacterial cell division protein, rnp domain, cell division, transmembrane, inner membrane
• Biological source: ESCHERICHIA COLI
• Cellular location: Cell inner membrane ; Single-pass type II membrane protein : P29131
• Total number of polymer chains: 1
• Total formula weight: 8928.04

Authors

Yang, J.-C.,van den Ent, F.,Neuhaus, D.,Brevier, J.,Lowe, J. (deposition date: 2003-12-04, release date: 2004-09-24, Last modification date: 2024-05-15)

Primary citation

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

Experimental method

SOLUTION NMR