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2fok

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(New page: 200px<br /><applet load="2fok" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fok, resolution 2.30&Aring;" /> '''STRUCTURE OF RESTRIC...)
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[[Image:2fok.jpg|left|200px]]<br /><applet load="2fok" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2fok, resolution 2.30&Aring;" />
 
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'''STRUCTURE OF RESTRICTION ENDONUCLEASE FOKI'''<br />
 
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==Overview==
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==STRUCTURE OF RESTRICTION ENDONUCLEASE FOKI==
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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.
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<StructureSection load='2fok' size='340' side='right'caption='[[2fok]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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== Function ==
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[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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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2FOK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Planomicrobium_okeanokoites Planomicrobium okeanokoites]. Active as [http://en.wikipedia.org/wiki/Type_II_site-specific_deoxyribonuclease Type II site-specific deoxyribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.4 3.1.21.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FOK OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9724743 9724743]
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</div>
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[[Category: Planomicrobium okeanokoites]]
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<div class="pdbe-citations 2fok" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Type II site-specific deoxyribonuclease]]
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[[Category: Aggarwal, A.K.]]
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[[Category: Bitinaite, J.]]
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[[Category: Schildkraut, I.]]
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[[Category: Wah, D.A.]]
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[[Category: deoxyribonuclease]]
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[[Category: dna cleavage]]
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[[Category: dna hydrolysis]]
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[[Category: dna-binding protein]]
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[[Category: metal ion catalysis]]
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[[Category: metalloenzyme]]
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[[Category: nucleic acid recognition]]
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[[Category: type iis restriction endonuclease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:39:53 2007''
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==See Also==
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*[[Endonuclease 3D structures|Endonuclease 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Planomicrobium okeanokoites]]
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[[Category: Aggarwal AK]]
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[[Category: Bitinaite J]]
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[[Category: Schildkraut I]]
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[[Category: Wah DA]]

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STRUCTURE OF RESTRICTION ENDONUCLEASE FOKI

PDB ID 2fok

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