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1ev7

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[[Image:1ev7.gif|left|200px]]
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{{Seed}}
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[[Image:1ev7.png|left|200px]]
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{{STRUCTURE_1ev7| PDB=1ev7 | SCENE= }}
{{STRUCTURE_1ev7| PDB=1ev7 | SCENE= }}
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'''CRYSTAL STRUCTURE OF DNA RESTRICTION ENDONUCLEASE NAEI'''
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===CRYSTAL STRUCTURE OF DNA RESTRICTION ENDONUCLEASE NAEI===
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==Overview==
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NAE:I is transformed from DNA endonuclease to DNA topoisomerase and recombinase by a single amino acid substitution. The crystal structure of NAE:I was solved at 2.3 A resolution and shows that NAE:I is a dimeric molecule with two domains per monomer. Each domain contains one potential DNA recognition motif corresponding to either endonuclease or topoisomerase activity. The N-terminal domain core folds like the other type II restriction endonucleases as well as lambda-exonuclease and the DNA repair enzymes MutH and Vsr, implying a common evolutionary origin and catalytic mechanism. The C-terminal domain contains a catabolite activator protein (CAP) motif present in many DNA-binding proteins, including the type IA and type II topoisomerases. Thus, the NAE:I structure implies that DNA processing enzymes evolved from a few common ancestors. NAE:I may be an evolutionary bridge between endonuclease and DNA processing enzymes.
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(as it appears on PubMed at http://www.pubmed.gov), where 10856254 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10856254}}
==About this Structure==
==About this Structure==
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[[Category: Restriction endonuclease]]
[[Category: Restriction endonuclease]]
[[Category: Topoisomerase]]
[[Category: Topoisomerase]]
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Revision as of 23:04, 30 June 2008

Template:STRUCTURE 1ev7

CRYSTAL STRUCTURE OF DNA RESTRICTION ENDONUCLEASE NAEI

Template:ABSTRACT PUBMED 10856254

About this Structure

1EV7 is a Single protein structure of sequence from Lechevalieria aerocolonigenes. Full crystallographic information is available from OCA.

Reference

Crystal structure of NaeI-an evolutionary bridge between DNA endonuclease and topoisomerase., Huai Q, Colandene JD, Chen Y, Luo F, Zhao Y, Topal MD, Ke H, EMBO J. 2000 Jun 15;19(12):3110-8. PMID:10856254

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