This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1cmb
From Proteopedia
|
THREE DIMENSIONAL CRYSTAL STRUCTURES OF ESCHERICHIA COLI MET REPRESSOR WITH AND WITHOUT COREPRESSOR
Overview
The three-dimensional crystal structure of met repressor, in the presence, or absence of bound corepressor (S-adenosylmethionine), shows a dimer of, intertwined monomers, which do not have the helix-turn-helix motif, characteristic of other bacterial repressor and activator structures. We, propose that the interaction of met repressor with DNA occurs through, either a pair of symmetry-related alpha-helices or a pair of beta-strands, and suggest a model for binding of several dimers to met operator regions.
About this Structure
1CMB is a Single protein structure of sequence from Escherichia coli with PO4 as ligand. Full crystallographic information is available from OCA.
Reference
Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor., Rafferty JB, Somers WS, Saint-Girons I, Phillips SE, Nature. 1989 Oct 26;341(6244):705-10. PMID:2677753
Page seeded by OCA on Tue Nov 20 12:34:43 2007
