1fok

STRUCTURE OF RESTRICTION ENDONUCLEASE FOKI BOUND TO DNA

spinqualitylabelsall models 1fok, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1fok is a 3 chain structure with sequence from Planomicrobium okeanokoites. The December 2014 RCSB PDB Molecule of the Month feature on TAL Effectors by David Goodsell is 10.2210/rcsb_pdb/mom_2014_12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: FOKI (Planomicrobium okeanokoites) Resources: FirstGlance, OCA, RCSB, PDBsum Function [T2F1_FLAOK] Recognizes the double-stranded sequences GGATG and CATCC and cleaves respectively 14 bases after G-1 and 13 bases before C-1. 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Endonuclease

Proteopedia Page Contributors and Editors (what is this?)

OCA