1cfr
From Proteopedia
(New page: 200px<br /><applet load="1cfr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cfr, resolution 2.15Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1cfr.gif|left|200px]]<br /><applet load="1cfr" size=" | + | [[Image:1cfr.gif|left|200px]]<br /><applet load="1cfr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cfr, resolution 2.15Å" /> | caption="1cfr, resolution 2.15Å" /> | ||
'''CRYSTAL STRUCTURE OF CITROBACTER FREUNDII RESTRICTION ENDONUCLEASE CFR10I AT 2.15 ANGSTROMS RESOLUTION.'''<br /> | '''CRYSTAL STRUCTURE OF CITROBACTER FREUNDII RESTRICTION ENDONUCLEASE CFR10I AT 2.15 ANGSTROMS RESOLUTION.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The X-ray crystal structure of Citrobacter freundii restriction | + | The X-ray crystal structure of Citrobacter freundii restriction endonuclease Cfr10I has been determined at a resolution of 2.15 A by multiple isomorphous replacement methods and refined to an R-factor of 19.64%. The structure of Cfr10I represents the first structure of a restriction endonuclease recognizing a degenerated nucleotide sequence. Structural comparison of Cfr10I with previously solved structures of other restriction enzymes suggests that recognition of specific sequence occurs through contacts in the major and the minor grooves of DNA. The arrangement of the putative active site residues shows some striking differences from previously described restriction endonucleases and supports a two-metal-ion mechanism of catalysis. |
==About this Structure== | ==About this Structure== | ||
| - | 1CFR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii]. 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:// | + | 1CFR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii]. 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=1CFR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: restriction enzyme]] | [[Category: restriction enzyme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:05:37 2008'' |
Revision as of 10:05, 21 February 2008
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CRYSTAL STRUCTURE OF CITROBACTER FREUNDII RESTRICTION ENDONUCLEASE CFR10I AT 2.15 ANGSTROMS RESOLUTION.
Overview
The X-ray crystal structure of Citrobacter freundii restriction endonuclease Cfr10I has been determined at a resolution of 2.15 A by multiple isomorphous replacement methods and refined to an R-factor of 19.64%. The structure of Cfr10I represents the first structure of a restriction endonuclease recognizing a degenerated nucleotide sequence. Structural comparison of Cfr10I with previously solved structures of other restriction enzymes suggests that recognition of specific sequence occurs through contacts in the major and the minor grooves of DNA. The arrangement of the putative active site residues shows some striking differences from previously described restriction endonucleases and supports a two-metal-ion mechanism of catalysis.
About this Structure
1CFR is a Single protein structure of sequence from Citrobacter freundii. 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 Citrobacter freundii restriction endonuclease Cfr10I at 2.15 A resolution., Bozic D, Grazulis S, Siksnys V, Huber R, J Mol Biol. 1996 Jan 12;255(1):176-86. PMID:8568865
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