1eop

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eop OCA], [https://pdbe.org/1eop PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eop RCSB], [https://www.ebi.ac.uk/pdbsum/1eop PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eop ProSAT]</span></td></tr>

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== 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<ref>PMID:10801972</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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