1eoo: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[1eoo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EOO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EOO FirstGlance]. <br>
-</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=1eoo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eoo OCA], [https://pdbe.org/1eoo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eoo RCSB], [https://www.ebi.ac.uk/pdbsum/1eoo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eoo ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.16&#8491;</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=1eoo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eoo OCA], [https://pdbe.org/1eoo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eoo RCSB], [https://www.ebi.ac.uk/pdbsum/1eoo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eoo ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/T2E5_ECOLX T2E5_ECOLX] Recognizes the double-stranded sequence GATATC and cleaves after T-3.
-<div style="background-color:#fffaf0;">
-== 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>
-</div>
-<div class="pdbe-citations 1eoo" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Endonuclease 3D structures|Endonuclease 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>