2fkh: Difference between revisions

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[[Image:2fkh.gif|left|200px]]
{{Seed}}
[[Image:2fkh.png|left|200px]]


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{{STRUCTURE_2fkh|  PDB=2fkh  |  SCENE=  }}  
{{STRUCTURE_2fkh|  PDB=2fkh  |  SCENE=  }}  


'''Crystal Form II of Pre-Reactive Complex of Restriction Endonuclease HinP1I with Cognate DNA and Calcium Ions'''
===Crystal Form II of Pre-Reactive Complex of Restriction Endonuclease HinP1I with Cognate DNA and Calcium Ions===




==Overview==
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HinP1I recognizes and cleaves the palindromic tetranucleotide sequence G downward arrowCGC in DNA. We report three structures of HinP1I-DNA complexes: in the presence of Ca(2+) (pre-reactive complex), in the absence of metal ion (binary complex) and in the presence of Mg(2+) (post-reactive complex). HinP1I forms a back-to-back dimer with two active sites and two DNA duplexes bound on the outer surfaces of the dimer facing away from each other. The 10 bp DNA duplexes undergo protein-induced distortions exhibiting features of A-, B- and Z-conformations: bending on one side (by intercalation of a phenylalanine side chain into the major groove), base flipping on the other side of the recognition site (by expanding the step rise distance of the local base pair to Z-form) and a local A-form conformation between the two central C:G base pairs of the recognition site (by binding of the N-terminal helix in the minor groove). In the pre- and post-reactive complexes, two metals (Ca(2+) or Mg(2+)) are found in the active site. The enzyme appears to cleave DNA sequentially, hydrolyzing first one DNA strand, as seen in the post-reactive complex in the crystalline state, and then the other, as supported by the observation that, in solution, a nicked DNA intermediate accumulates before linearization.
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{{ABSTRACT_PUBMED_16473850}}


==About this Structure==
==About this Structure==
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[[Category: Protein-dna-metal ion complex]]
[[Category: Protein-dna-metal ion complex]]
[[Category: Restriction endonuclease]]
[[Category: Restriction endonuclease]]
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