1fok
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fok]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Planomicrobium_okeanokoites Planomicrobium okeanokoites]. The December 2014 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''TAL Effectors'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2014_12 10.2210/rcsb_pdb/mom_2014_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FOK FirstGlance]. <br> | <table><tr><td colspan='2'>[[1fok]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Planomicrobium_okeanokoites Planomicrobium okeanokoites]. The December 2014 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''TAL Effectors'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2014_12 10.2210/rcsb_pdb/mom_2014_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FOK 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=1fok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fok OCA], [https://pdbe.org/1fok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fok RCSB], [https://www.ebi.ac.uk/pdbsum/1fok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fok 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]] 2.8Å</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=1fok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fok OCA], [https://pdbe.org/1fok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fok RCSB], [https://www.ebi.ac.uk/pdbsum/1fok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fok ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/T2F1_PLAOK T2F1_PLAOK] Recognizes the double-stranded sequence 5'-GGATG-3'/3'-CATCC-5' and cleaves respectively 14 bases after G-1 and 13 bases before C-1. | [https://www.uniprot.org/uniprot/T2F1_PLAOK T2F1_PLAOK] Recognizes the double-stranded sequence 5'-GGATG-3'/3'-CATCC-5' and cleaves respectively 14 bases after G-1 and 13 bases before C-1. | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | FokI is a member of an unusual class of bipartite restriction enzymes that recognize a specific DNA sequence and cleave DNA nonspecifically a short distance away from that sequence. Because of its unusual bipartite nature, FokI has been used to create artificial enzymes with new specificities. We have determined the crystal structure at 2.8A resolution of the complete FokI enzyme bound to DNA. As anticipated, the enzyme contains amino- and carboxy-terminal domains corresponding to the DNA-recognition and cleavage functions, respectively. The recognition domain is made of three smaller subdomains (D1, D2 and D3) which are evolutionarily related to the helix-turn-helix-containing DNA-binding domain of the catabolite gene activator protein CAP. The CAP core has been extensively embellished in the first two subdomains, whereas in the third subdomain it has been co-opted for protein-protein interactions. Surprisingly, the cleavage domain contains only a single catalytic centre, raising the question of how monomeric FokI manages to cleave both DNA strands. Unexpectedly, the cleavage domain is sequestered in a 'piggyback' fashion by the recognition domain. The structure suggests a new mechanism for nuclease activation and provides a framework for the design of chimaeric enzymes with altered specificities. | ||
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| - | Structure of the multimodular endonuclease FokI bound to DNA.,Wah DA, Hirsch JA, Dorner LF, Schildkraut I, Aggarwal AK Nature. 1997 Jul 3;388(6637):97-100. PMID:9214510<ref>PMID:9214510</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1fok" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Endonuclease 3D structures|Endonuclease 3D structures]] | *[[Endonuclease 3D structures|Endonuclease 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
STRUCTURE OF RESTRICTION ENDONUCLEASE FOKI BOUND TO DNA
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