1ynm
From Proteopedia
(New page: 200px<br /><applet load="1ynm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ynm, resolution 2.65Å" /> '''Crystal structure of...) |
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| - | [[Image:1ynm.gif|left|200px]]<br /><applet load="1ynm" size=" | + | [[Image:1ynm.gif|left|200px]]<br /><applet load="1ynm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ynm, resolution 2.65Å" /> | caption="1ynm, resolution 2.65Å" /> | ||
'''Crystal structure of restriction endonuclease HinP1I'''<br /> | '''Crystal structure of restriction endonuclease HinP1I'''<br /> | ||
==Overview== | ==Overview== | ||
| - | HinP1I, a type II restriction endonuclease, recognizes and cleaves a | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1YNM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Active as [http://en.wikipedia.org/wiki/Type_II_site-specific_deoxyribonuclease Type II site-specific deoxyribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.4 3.1.21.4] Full crystallographic information is available from [http:// | + | 1YNM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Active as [http://en.wikipedia.org/wiki/Type_II_site-specific_deoxyribonuclease Type II site-specific deoxyribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.4 3.1.21.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YNM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Type II site-specific deoxyribonuclease]] | [[Category: Type II site-specific deoxyribonuclease]] | ||
[[Category: Cheng, X.]] | [[Category: Cheng, X.]] | ||
| - | [[Category: Horton, J | + | [[Category: Horton, J R.]] |
[[Category: Maunus, R.]] | [[Category: Maunus, R.]] | ||
| - | [[Category: Roberts, R | + | [[Category: Roberts, R J.]] |
| - | [[Category: Wilson, G | + | [[Category: Wilson, G G.]] |
[[Category: Yang, Z.]] | [[Category: Yang, Z.]] | ||
[[Category: dimerizaton]] | [[Category: dimerizaton]] | ||
[[Category: restriction endonuclease]] | [[Category: restriction endonuclease]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:07:14 2008'' |
Revision as of 14:07, 21 February 2008
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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.
About this Structure
1YNM is a Single protein structure of sequence from Haemophilus influenzae. Active as Type II site-specific deoxyribonuclease, with EC number 3.1.21.4 Full crystallographic information is available from OCA.
Reference
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
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