1EV0

SOLUTION STRUCTURE OF THE MINE TOPOLOGICAL SPECIFICITY DOMAIN

Summary for 1EV0

• Entry DOI: 10.2210/pdb1ev0/pdb
• Descriptor: MINE (1 entity in total)
• Functional Keywords: mine, topological specificity, cell division, mincd, minicell, cell cycle
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 13427.31

Authors

King, G.F.,Maciejewski, M.W.,Pan, B.,Mullen, G.P. (deposition date: 2000-04-19, release date: 2000-11-01, Last modification date: 2024-05-22)

Primary citation

King, G.F.,Shih, Y.L.,Maciejewski, M.W.,Bains, N.P.,Pan, B.,Rowland, S.L.,Mullen, G.P.,Rothfield, L.I.
Structural basis for the topological specificity function of MinE.
Nat.Struct.Biol., 7:1013-1017, 2000

PubMed Abstract: Correct positioning of the division septum in Escherichia coli depends on the coordinated action of the MinC, MinD and MinE proteins. Topological specificity is conferred on the MinCD division inhibitor by MinE, which counters MinCD activity only in the vicinity of the preferred midcell division site. Here we report the structure of the homodimeric topological specificity domain of Escherichia coli MinE and show that it forms a novel alphabeta sandwich. Structure-directed mutagenesis of conserved surface residues has enabled us to identify a spatially restricted site on the surface of the protein that is critical for the topological specificity function of MinE.

PubMed: 11062554
DOI: 10.1038/80917

Experimental method

SOLUTION NMR