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Updated: Jun 20, 2026

Genetic Modification of Cyanobacteria by Conjugation Using the CyanoGate Modular Cloning Toolkit

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Published on: October 31, 2019

Structure of the restriction-modification controller protein C.Esp1396I.

N Ball¹, S D Streeter, G G Kneale

¹Biophysics Laboratories, Institute of Biomedical and Biomolecular Sciences, School of Biological Sciences, University of Portsmouth, Portsmouth, UK.

Acta Crystallographica. Section D, Biological Crystallography

|August 20, 2009

Summary

This summary is machine-generated.

The Esp1396I restriction-modification controller protein

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Area of Science:

Molecular Biology
Structural Biology
Biochemistry

Background:

The Esp1396I restriction-modification (R-M) system regulates gene expression via a controller protein.
Previous studies determined the structure of the protein bound to DNA, but not the free protein.

Purpose of the Study:

To determine the crystal structure of the free Esp1396I controller protein.
To investigate conformational changes upon DNA binding.

Main Methods:

X-ray crystallography was used to determine the structure of the free protein.
The structure of a mutant protein (R35A) was also determined.
Comparison of free and DNA-bound protein structures.

Main Results:

The crystal structure of the free Esp1396I controller protein was determined, revealing seven dimers in the asymmetric unit.
Two monomers exhibited alternative conformations in the loop region flanking the DNA-recognition helix.
These alternative conformations were also observed in the R35A mutant.
A 1.4 A displacement of recognition helices was observed upon DNA binding.

Conclusions:

The alternative conformations of the free protein may contribute to DNA-sequence promiscuity.
Conformational changes occur upon DNA binding, involving the recognition helices.