View source for 2fok


==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.
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== 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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2fok" style="background-color:#fffaf0;"></div>

==See Also==
*[[Endonuclease 3D structures|Endonuclease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Planomicrobium okeanokoites]]
[[Category: Aggarwal AK]]
[[Category: Bitinaite J]]
[[Category: Schildkraut I]]
[[Category: Wah DA]]