1eoo: Difference between revisions

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<StructureSection load='1eoo' size='340' side='right'caption='[[1eoo]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
<StructureSection load='1eoo' size='340' side='right'caption='[[1eoo]], [[Resolution|resolution]] 2.16&Aring;' 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 [https://proteopedia.org/fgij/fg.htm?mol=1EOO FirstGlance]. <br>
<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='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>
</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>
<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.  
[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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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Type II site-specific deoxyribonuclease]]
[[Category: Horton NC]]
[[Category: Horton, N C]]
[[Category: Perona JJ]]
[[Category: Perona, J J]]
[[Category: Endonuclease]]
[[Category: Hydrolase-dna complex]]
[[Category: Induced fit]]
[[Category: Protein-dna recognition]]

Revision as of 13:24, 21 December 2022

ECORV BOUND TO COGNATE DNAECORV BOUND TO COGNATE DNA

Structural highlights

1eoo is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

T2E5_ECOLX Recognizes the double-stranded sequence GATATC and cleaves after T-3.

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[1]

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

See Also

References

  1. 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

1eoo, resolution 2.16Å

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OCA