1GHH

SOLUTION STRUCTURE OF DINI

Replaces:  1F0A

Summary for 1GHH

• Entry DOI: 10.2210/pdb1ghh/pdb
• Descriptor: DNA-DAMAGE-INDUCIBLE PROTEIN I (1 entity in total)
• Functional Keywords: bicelle, dini, dipolar coupling, liquid crystal, pf1, reca, protein binding
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 8957.94

Authors

Ramirez, B.E.,Voloshin, O.N.,Camerini-Otero, R.D.,Bax, A. (deposition date: 2000-12-19, release date: 2001-01-10, Last modification date: 2023-12-27)

Primary citation

Ramirez, B.E.,Voloshin, O.N.,Camerini-Otero, R.D.,Bax, A.
Solution structure of DinI provides insight into its mode of RecA inactivation.
Protein Sci., 9:2161-2169, 2000

PubMed 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.

PubMed: 11152126

Experimental method

SOLUTION NMR