1uta
From Proteopedia
SOLUTION STRUCTURE OF THE C-TERMINAL RNP DOMAIN FROM THE DIVISOME PROTEIN FTSN
Overview
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.
About this Structure
1UTA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Solution structure and domain architecture of the divisome protein FtsN., Yang JC, Van Den Ent F, Neuhaus D, Brevier J, Lowe J, Mol Microbiol. 2004 May;52(3):651-60. PMID:15101973 Page seeded by OCA on Sat May 3 11:39:33 2008
