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1pvu

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(New page: 200px<br /><applet load="1pvu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pvu, resolution 2.4&Aring;" /> '''THE CRYSTAL STRUCTURE...)
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[[Image:1pvu.jpg|left|200px]]<br /><applet load="1pvu" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1pvu, resolution 2.4&Aring;" />
caption="1pvu, resolution 2.4&Aring;" />
'''THE CRYSTAL STRUCTURE OF PVUII ENDONUCLEASE REVEALS EXTENSIVE STRUCTURAL HOMOLOGIES TO ECORV'''<br />
'''THE CRYSTAL STRUCTURE OF PVUII ENDONUCLEASE REVEALS EXTENSIVE STRUCTURAL HOMOLOGIES TO ECORV'''<br />
==Overview==
==Overview==
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The crystal structure of the dimeric PvuII restriction endonuclease, (R.PvuII) has been determined at a resolution of 2.4A. The protein has a, mixed alpha/beta architecture and consists of two subdomains. Despite a, lack of sequence homology, extensive structural similarities exist between, one R.PvuII subdomain and the DNA-binding subdomain of EcoRV endonuclease, (R.EcoRV); the dimerization subdomains are unrelated. Within the similar, domains, flexible segments of R.PvuII are topologically equivalent to the, DNA-binding turns of R.EcoRV; potential catalytic residues can be deduced, from the structural similarities to R.EcoRV. Conformational flexibility is, important for the interaction with DNA. A possible classification of, endonuclease structures on the basis of the positions of the scissile, phosphates is discussed.
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The crystal structure of the dimeric PvuII restriction endonuclease (R.PvuII) has been determined at a resolution of 2.4A. The protein has a mixed alpha/beta architecture and consists of two subdomains. Despite a lack of sequence homology, extensive structural similarities exist between one R.PvuII subdomain and the DNA-binding subdomain of EcoRV endonuclease (R.EcoRV); the dimerization subdomains are unrelated. Within the similar domains, flexible segments of R.PvuII are topologically equivalent to the DNA-binding turns of R.EcoRV; potential catalytic residues can be deduced from the structural similarities to R.EcoRV. Conformational flexibility is important for the interaction with DNA. A possible classification of endonuclease structures on the basis of the positions of the scissile phosphates is discussed.
==About this Structure==
==About this Structure==
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1PVU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PVU OCA].
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1PVU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]. 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=1PVU OCA].
==Reference==
==Reference==
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[[Category: type ii restriction endonuclease]]
[[Category: type ii restriction endonuclease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:10:01 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:33:02 2008''

Revision as of 12:33, 21 February 2008

Image:1pvu.jpg

1pvu, resolution 2.4Å

Drag the structure with the mouse to rotate

THE CRYSTAL STRUCTURE OF PVUII ENDONUCLEASE REVEALS EXTENSIVE STRUCTURAL HOMOLOGIES TO ECORV

Overview

The crystal structure of the dimeric PvuII restriction endonuclease (R.PvuII) has been determined at a resolution of 2.4A. The protein has a mixed alpha/beta architecture and consists of two subdomains. Despite a lack of sequence homology, extensive structural similarities exist between one R.PvuII subdomain and the DNA-binding subdomain of EcoRV endonuclease (R.EcoRV); the dimerization subdomains are unrelated. Within the similar domains, flexible segments of R.PvuII are topologically equivalent to the DNA-binding turns of R.EcoRV; potential catalytic residues can be deduced from the structural similarities to R.EcoRV. Conformational flexibility is important for the interaction with DNA. A possible classification of endonuclease structures on the basis of the positions of the scissile phosphates is discussed.

About this Structure

1PVU is a Single protein structure of sequence from Proteus vulgaris. Active as Type II site-specific deoxyribonuclease, with EC number 3.1.21.4 Full crystallographic information is available from OCA.

Reference

Crystal structure of PvuII endonuclease reveals extensive structural homologies to EcoRV., Athanasiadis A, Vlassi M, Kotsifaki D, Tucker PA, Wilson KS, Kokkinidis M, Nat Struct Biol. 1994 Jul;1(7):469-75. PMID:7664066

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