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[[Image:2fok.jpg|left|200px]]
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{{STRUCTURE_2fok|  PDB=2fok  |  SCENE=  }}
'''STRUCTURE OF RESTRICTION ENDONUCLEASE FOKI'''


==STRUCTURE OF RESTRICTION ENDONUCLEASE FOKI==
<StructureSection load='2fok' size='340' side='right'caption='[[2fok]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2fok]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Planomicrobium_okeanokoites Planomicrobium okeanokoites]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FOK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#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=2fok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fok OCA], [https://pdbe.org/2fok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fok RCSB], [https://www.ebi.ac.uk/pdbsum/2fok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fok ProSAT]</span></td></tr>
</table>
== 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
FokI is a member an unusual class of restriction enzymes that recognize a specific DNA sequence and cleave nonspecifically a short distance away from that sequence. FokI consists of an N-terminal DNA recognition domain and a C-terminal cleavage domain. The bipartite nature of FokI has led to the development of artificial enzymes with novel specificities. We have solved the structure of FokI to 2.3 A resolution. The structure reveals a dimer, in which the dimerization interface is mediated by the cleavage domain. Each monomer has an overall conformation similar to that found in the FokI-DNA complex, with the cleavage domain packing alongside the DNA recognition domain. In corroboration with the cleavage data presented in the accompanying paper in this issue of Proceedings, we propose a model for FokI DNA cleavage that requires the dimerization of FokI on DNA to cleave both DNA strands.


==Overview==
Structure of FokI has implications for DNA cleavage.,Wah DA, Bitinaite J, Schildkraut I, Aggarwal AK Proc Natl Acad Sci U S A. 1998 Sep 1;95(18):10564-9. PMID:9724743<ref>PMID:9724743</ref>
FokI is a member an unusual class of restriction enzymes that recognize a specific DNA sequence and cleave nonspecifically a short distance away from that sequence. FokI consists of an N-terminal DNA recognition domain and a C-terminal cleavage domain. The bipartite nature of FokI has led to the development of artificial enzymes with novel specificities. We have solved the structure of FokI to 2.3 A resolution. The structure reveals a dimer, in which the dimerization interface is mediated by the cleavage domain. Each monomer has an overall conformation similar to that found in the FokI-DNA complex, with the cleavage domain packing alongside the DNA recognition domain. In corroboration with the cleavage data presented in the accompanying paper in this issue of Proceedings, we propose a model for FokI DNA cleavage that requires the dimerization of FokI on DNA to cleave both DNA strands.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2FOK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Planomicrobium_okeanokoites Planomicrobium okeanokoites]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FOK OCA].
</div>
<div class="pdbe-citations 2fok" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structure of FokI has implications for DNA cleavage., Wah DA, Bitinaite J, Schildkraut I, Aggarwal AK, Proc Natl Acad Sci U S A. 1998 Sep 1;95(18):10564-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9724743 9724743]
*[[Endonuclease 3D structures|Endonuclease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Planomicrobium okeanokoites]]
[[Category: Planomicrobium okeanokoites]]
[[Category: Single protein]]
[[Category: Aggarwal AK]]
[[Category: Type II site-specific deoxyribonuclease]]
[[Category: Bitinaite J]]
[[Category: Aggarwal, A K.]]
[[Category: Schildkraut I]]
[[Category: Bitinaite, J.]]
[[Category: Wah DA]]
[[Category: Schildkraut, I.]]
[[Category: Wah, D A.]]
[[Category: Deoxyribonuclease]]
[[Category: Dna cleavage]]
[[Category: Dna hydrolysis]]
[[Category: Dna-binding protein]]
[[Category: Metal ion catalysis]]
[[Category: Metalloenzyme]]
[[Category: Nucleic acid recognition]]
[[Category: Type iis restriction endonuclease]]
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Retrieved from "https://proteopedia.org/2fok"