Dimerization allows DNA target site recognition by the NarL response regulator

Two-component signal transduction systems are modular phosphorelay regulatory pathways common in prokaryotes. In the co-crystal structure of the Escherichia coli NarL signal output domain bound to DNA, we observe how the NarL family of two-component response regulators can bind DNA. DNA recognition...

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Bibliographic Details
Published in:Nature Structural Biology Vol. 9; no. 10; pp. 771 - 778
Main Authors: Maris, Ann E., Sawaya, Michael R., Kaczor-Grzeskowiak, Maria, Jarvis, Michael R., Bearson, Shawn M.D., Kopka, Mary L., Schröder, Imke, Gunsalus, Robert P., Dickerson, Richard E.
Format: Journal Article
Language:English
Published: New York Nature Publishing Group US 01.10.2002
Nature Publishing Group
Subjects:
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Biochemistry
Biological Microscopy
Biomedical and Life Sciences
Cloning, Molecular
Crystallography, X-Ray
Deoxyribonucleic acid
Dimerization
DNA
DNA - chemistry
DNA - metabolism
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - metabolism
E coli
Escherichia coli
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - metabolism
Life Sciences
Membrane Biology
Nucleic Acid Conformation
Promoter Regions, Genetic
Protein Binding
Protein Conformation
Protein Structure
Protein Structure, Secondary
Recombinant Proteins - chemistry
Structure-Activity Relationship
ISSN:1072-8368, 1545-9993, 1545-9985
Online Access:Get full text
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Summary:Two-component signal transduction systems are modular phosphorelay regulatory pathways common in prokaryotes. In the co-crystal structure of the Escherichia coli NarL signal output domain bound to DNA, we observe how the NarL family of two-component response regulators can bind DNA. DNA recognition is accompanied by the formation of a new dimerization interface, which could occur only in the full-length protein via a large intramolecular domain rearrangement. The DNA is recognized by the concerted effects of solvation, van der Waals forces and inherent DNA deformability, rather than determined primarily by major groove hydrogen bonding. These subtle forces permit a small DNA-binding domain to perturb the DNA helix, leading to major DNA curvature and a transition from B- to A-form DNA at the binding site, where valine on the recognition helix interacts unexpectedly with the polar major groove floor.
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ISSN:1072-8368
1545-9993
1545-9985
DOI:10.1038/nsb845