1EOP

ECORV BOUND TO COGNATE DNA

Summary for 1EOP

• Entry DOI: 10.2210/pdb1eop/pdb
• Descriptor: DNA (5'-D(*GP*AP*AP*GP*AP*TP*AP*TP*CP*TP*TP*C)-3'), TYPE II RESTRICTION ENZYME ECORV (3 entities in total)
• Functional Keywords: protein-dna recognition, induced fit, endonuclease, hydrolase-dna complex, hydrolase/dna
• Biological source: Escherichia coli
• Total number of polymer chains: 4
• Total formula weight: 64751.59

Authors

Horton, N.C.,Perona, J.J. (deposition date: 2000-03-23, release date: 2000-04-04, Last modification date: 2024-02-07)

Primary citation

Horton, N.C.,Perona, J.J.
Crystallographic snapshots along a protein-induced DNA-bending pathway.
Proc.Natl.Acad.Sci.USA, 97:5729-5734, 2000

PubMed Abstract: Two new high-resolution cocrystal structures of EcoRV endonuclease bound to DNA show that a large variation in DNA-bending angles is sampled in the ground state binary complex. Together with previous structures, these data reveal a contiguous series of protein conformational states delineating a specific trajectory for the induced-fit pathway. Rotation of the DNA-binding domains, together with movements of two symmetry-related helices binding in the minor groove, causes base unstacking at a key base-pair step and propagates structural changes that assemble the active sites. These structures suggest a complex mechanism for DNA bending that depends on forces generated by interacting protein segments, and on selective neutralization of phosphate charges along the inner face of the bent double helix.

PubMed: 10801972
DOI: 10.1073/pnas.090370797

Experimental method

X-RAY DIFFRACTION (2.6 Å)