1uta

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

spinqualitylabelsall models 1uta Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1uta is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FTSN_ECOLI Essential cell division protein. May play a role in the assembly or stability of the septation machinery. May interact with FtsA, PBP3 and FtsQ. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA