 |
PDBsum entry 1f0a
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Protein binding
|
PDB id
|
|
|
|
1f0a
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Solution structure of dini provides insight into its mode of reca inactivation.
|
|
|
Authors
|
|
B.E.Ramirez,
O.N.Voloshin,
R.D.Camerini-Otero,
A.Bax.
|
|
|
Ref.
|
|
Protein Sci, 2000,
9,
2161-2169.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
perfect match.
|
|
|
|
Abstract
|
|
|
The Escherichia coli RecA protein triggers both DNA repair and mutagenesis in a
process known as the SOS response. The 81-residue E. coli protein DinI inhibits
activity of RecA in vivo. The solution structure of DinI has been determined by
multidimensional triple resonance NMR spectroscopy, using restraints derived
from two sets of residual dipolar couplings, obtained in bicelle and phage
media, supplemented with J couplings and a moderate number of NOE restraints.
DinI has an alpha/beta fold comprised of a three-stranded beta-sheet and two
alpha-helices. The beta-sheet topology is unusual: the central strand is flanked
by a parallel and an antiparallel strand and the sheet is remarkably flat. The
structure of DinI shows that six negatively charged Glu and Asp residues on
DinI's kinked C-terminal alpha-helix form an extended, negatively charged ridge.
We propose that this ridge mimics the electrostatic character of the DNA
phospodiester backbone, thereby enabling DinI to compete with single-stranded
DNA for RecA binding. Biochemical data confirm that DinI is able to displace
ssDNA from RecA.
|
|
|
|
|
|
|
