Lac repressor genetic map in real space.
Here, we present a graphic display of the phenotypes of more than 4000 single amino acid substitution mutations on the three-dimensional structure of the lac repressor tetramer bound to DNA. The genetic data and the X-ray diffraction studies contribute to define an allosteric mechanism and yield a visual demonstration of the importance of core or buried residues in protein structure.
Pace
H C
HC
Department of Chemistry, University of Pennsylvania, Philadelphia, USA.
Kercher
M A
MA
Lu
P
P
Markiewicz
P
P
Miller
J H
JH
Chang
G
G
Lewis
M
M
D000495:Allosteric Site; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics*; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics; D029968:Escherichia coli Proteins; D056968:Lac Repressors; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation; D012097:Repressor Proteins / Q000737:chemistry / Q000235:genetics*
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D056968:Lac Repressors; C539064:LacI protein, E coli; D012097:Repressor Proteins