1cfr

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[[Image:1cfr.gif|left|200px]]
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{{STRUCTURE_1cfr| PDB=1cfr | SCENE= }}
{{STRUCTURE_1cfr| PDB=1cfr | SCENE= }}
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'''CRYSTAL STRUCTURE OF CITROBACTER FREUNDII RESTRICTION ENDONUCLEASE CFR10I AT 2.15 ANGSTROMS RESOLUTION.'''
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===CRYSTAL STRUCTURE OF CITROBACTER FREUNDII RESTRICTION ENDONUCLEASE CFR10I AT 2.15 ANGSTROMS RESOLUTION.===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8568865 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8568865}}
==About this Structure==
==About this Structure==
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[[Category: Restriction endonuclease]]
[[Category: Restriction endonuclease]]
[[Category: Restriction enzyme]]
[[Category: Restriction enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:41:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:41:24 2008''

Revision as of 17:41, 30 June 2008

Template:STRUCTURE 1cfr

CRYSTAL STRUCTURE OF CITROBACTER FREUNDII RESTRICTION ENDONUCLEASE CFR10I AT 2.15 ANGSTROMS RESOLUTION.

Template:ABSTRACT PUBMED 8568865

About this Structure

1CFR is a Single protein structure of sequence from Citrobacter freundii. 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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