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PMID: 9301333 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Review

Lac repressor genetic map in real space.

Trends in biochemical sciences ·Vol. 22 ·No. 9 ·1997-09-00 ·Pages 334-9

Pace HC, Kercher MA, Lu P, Markiewicz P, Miller JH, Chang G, Lewis M

Abstract

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.

MeSH Terms
Allosteric Site Bacterial Proteins/chemistry,genetics Escherichia coli/chemistry,genetics Escherichia coli Proteins Lac Repressors Models, Molecular Mutation Protein Conformation Repressor Proteins/chemistry,genetics
Chemicals
Bacterial Proteins Escherichia coli Proteins Lac Repressors LacI protein, E coli Repressor Proteins
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Pace H C
Department of Chemistry, University of Pennsylvania, Philadelphia, USA.
Kercher M A
Lu P
Markiewicz P
Miller J H
Chang G
Lewis M
Article Info
Journal
Trends in biochemical sciences
Abbr.
Trends Biochem Sci
ISSN
0968-0004
Published
1997-09-00
Pages
334-9
Language
English
Region
England
NLM ID
7610674
Subset
IM
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