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1eoo, resolution 2.16Å ()
Activity: Type II site-specific deoxyribonuclease, with EC number
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Publication Abstract from PubMed

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.

Crystallographic snapshots along a protein-induced DNA-bending pathway., Horton NC, Perona JJ, Proc Natl Acad Sci U S A. 2000 May 23;97(11):5729-34. PMID:10801972

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1eoo is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

See Also


  • Horton NC, Perona JJ. Crystallographic snapshots along a protein-induced DNA-bending pathway. Proc Natl Acad Sci U S A. 2000 May 23;97(11):5729-34. PMID:10801972 doi:10.1073/pnas.090370797

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