2fok: Difference between revisions
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New page: left|200px<br /><applet load="2fok" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fok, resolution 2.30Å" /> '''STRUCTURE OF RESTRIC... |
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== | ==STRUCTURE OF RESTRICTION ENDONUCLEASE FOKI== | ||
FokI is a member an unusual class of restriction enzymes that recognize a | <StructureSection load='2fok' size='340' side='right'caption='[[2fok]], [[Resolution|resolution]] 2.30Å' 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]] 2.3Å</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. | |||
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®/PubMed®, 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: Planomicrobium okeanokoites]] | ||
[[Category: Aggarwal AK]] | |||
[[Category: Bitinaite J]] | |||
[[Category: Aggarwal | [[Category: Schildkraut I]] | ||
[[Category: Bitinaite | [[Category: Wah DA]] | ||
[[Category: Schildkraut | |||
[[Category: Wah | |||
Latest revision as of 06:44, 9 August 2023
STRUCTURE OF RESTRICTION ENDONUCLEASE FOKI
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