Crystallographic snapshots along a protein-induced DNA-bending pathway

Nancy C Horton, John J. Perona

Research output: Contribution to journalArticle

42 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)5729-5734
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume97
Issue number11
DOIs
StatePublished - May 23 2000
Externally publishedYes

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DNA
Proteins
Base Pairing
Catalytic Domain
Phosphates
GATATC-specific type II deoxyribonucleases

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Crystallographic snapshots along a protein-induced DNA-bending pathway. / Horton, Nancy C; Perona, John J.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 97, No. 11, 23.05.2000, p. 5729-5734.

Research output: Contribution to journalArticle

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