1uta
From Proteopedia
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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
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