1ynm: Difference between revisions

Revision as of 12:54, 29 July 2008

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File:1ynm.png

Template:STRUCTURE 1ynm

Crystal structure of restriction endonuclease HinP1ICrystal structure of restriction endonuclease HinP1I

Template:ABSTRACT PUBMED 15805123

About this StructureAbout this Structure

1YNM is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.

ReferenceReference

Structure of HinP1I endonuclease reveals a striking similarity to the monomeric restriction enzyme MspI., Yang Z, Horton JR, Maunus R, Wilson GG, Roberts RJ, Cheng X, Nucleic Acids Res. 2005 Apr 1;33(6):1892-901. Print 2005. PMID:15805123

Page seeded by OCA on Tue Jul 29 12:54:44 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1ynm.gif|left|200px]]
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 {{STRUCTURE_1ynm|  PDB=1ynm  |  SCENE=  }}
-'''Crystal structure of restriction endonuclease HinP1I'''
+===Crystal structure of restriction endonuclease HinP1I===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15805123}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15805123 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15805123}}
 ==About this Structure==
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 [[Category: Dimerizaton]]
 [[Category: Restriction endonuclease]]
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