Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor.
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.
Rafferty
J B
JB
Astbury Department of Biophysics, University of Leeds, UK.
Somers
W S
WS
Saint-Girons
I
I
Phillips
S E
SE
D001059:Apoproteins; D001426:Bacterial Proteins; D001483:Base Sequence; D003460:Crystallization; D004269:DNA, Bacterial / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics*; D029968:Escherichia coli Proteins; D008958:Models, Molecular; D009875:Operator Regions, Genetic; D011487:Protein Conformation; D012097:Repressor Proteins; D012436:S-Adenosylmethionine / Q000235:genetics* / Q000378:metabolism; D014157:Transcription Factors
D001059:Apoproteins; D001426:Bacterial Proteins; D004269:DNA, Bacterial; D029968:Escherichia coli Proteins; C053317:MetJ protein, E coli; D012097:Repressor Proteins; D014157:Transcription Factors; D012436:S-Adenosylmethionine