1CMC

THREE DIMENSIONAL CRYSTAL STRUCTURES OF E. COLI MET REPRESSOR WITH AND WITHOUT COREPRESSOR

Summary for 1CMC

• Entry DOI: 10.2210/pdb1cmc/pdb
• Descriptor: MET REPRESSOR, MAGNESIUM ION, S-ADENOSYLMETHIONINE, ... (4 entities in total)
• Functional Keywords: dna-binding regulatory protein
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A8U6
• Total number of polymer chains: 2
• Total formula weight: 24900.60

Authors

Somers, W.S.,Phillips, S.E.V. (deposition date: 1992-08-28, release date: 1993-10-31, Last modification date: 2024-02-14)

Primary citation

Rafferty, J.B.,Somers, W.S.,Saint-Girons, I.,Phillips, S.E.
Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor.
Nature, 341:705-710, 1989

PubMed Abstract: 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.

PubMed: 2677753
DOI: 10.1038/341705a0

Experimental method

X-RAY DIFFRACTION (1.8 Å)