1eoo: Difference between revisions
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<StructureSection load='1eoo' size='340' side='right'caption='[[1eoo]], [[Resolution|resolution]] 2.16Å' scene=''> | <StructureSection load='1eoo' size='340' side='right'caption='[[1eoo]], [[Resolution|resolution]] 2.16Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1eoo]] is a 4 chain structure. 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 [ | <table><tr><td colspan='2'>[[1eoo]] is a 4 chain structure. 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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Type_II_site-specific_deoxyribonuclease Type II site-specific deoxyribonuclease], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.4 3.1.21.4] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Endonuclease|Endonuclease]] | *[[Endonuclease 3D structures|Endonuclease 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:14, 17 March 2021
ECORV BOUND TO COGNATE DNAECORV BOUND TO COGNATE DNA
Structural highlights
Function[T2E5_ECOLX] Recognizes the double-stranded sequence GATATC and cleaves after T-3. Publication Abstract from PubMedTwo 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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