1ynm: Difference between revisions

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[[Image:1ynm.gif|left|200px]]
{{Seed}}
[[Image:1ynm.png|left|200px]]


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{{STRUCTURE_1ynm|  PDB=1ynm  |  SCENE=  }}  
{{STRUCTURE_1ynm|  PDB=1ynm  |  SCENE=  }}  


'''Crystal structure of restriction endonuclease HinP1I'''
===Crystal structure of restriction endonuclease HinP1I===




==Overview==
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HinP1I, a type II restriction endonuclease, recognizes and cleaves a palindromic tetranucleotide sequence (G/CGC) in double-stranded DNA, producing 2 nt 5' overhanging ends. Here, we report the structure of HinP1I crystallized as one protein monomer in the crystallographic asymmetric unit. HinP1I displays an elongated shape, with a conserved catalytic core domain containing an active-site motif of SDX18QXK and a putative DNA-binding domain. Without significant sequence homology, HinP1I displays striking structural similarity to MspI, an endonuclease that cleaves a similar palindromic DNA sequence (C/CGG) and binds to that sequence crystallographically as a monomer. Almost all the structural elements of MspI can be matched in HinP1I, including both the DNA recognition and catalytic elements. Examining the protein-protein interactions in the crystal lattice, HinP1I could be dimerized through two helices located on the opposite side of the protein to the active site, generating a molecule with two active sites and two DNA-binding surfaces opposite one another on the outer surfaces of the dimer. A possible functional link between this unusual dimerization mode and the tetrameric restriction enzymes is discussed.
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==About this Structure==
==About this Structure==
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[[Category: Dimerizaton]]
[[Category: Dimerizaton]]
[[Category: Restriction endonuclease]]
[[Category: Restriction endonuclease]]
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