4b20: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4b20|  PDB=4b20  |  SCENE=  }}
===Structural basis of DNA loop recognition by Endonuclease V===
{{ABSTRACT_PUBMED_23313664}}


The entry 4b20 is ON HOLD until Paper Publication
==Function==
[[http://www.uniprot.org/uniprot/NFI_THEMA NFI_THEMA]] Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA. Acts in DNA repair. In vitro, can also cleave single-stranded substrates with inosine, double-stranded DNA with apurinic sites, or DNA sites with uracil or a mismatched base. When present in molar excess, two protein molecules can bind to the same DNA substrate and effect cleavage of both strands (in vitro).<ref>PMID:12081482</ref>  


Authors: Rosnes, I., Rowe, A.D., Forstrom, R.J., Alseth, I., Bjoras, M., Dalhus, B.
==About this Structure==
[[4b20]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B20 OCA].  


Description: Structural basis of DNA loop recognition by Endonuclease V
==Reference==
<references group="xtra"/><references/>
[[Category: Deoxyribonuclease V]]
[[Category: Thermotoga maritima]]
[[Category: Alseth, I.]]
[[Category: Bjoras, M.]]
[[Category: Dalhus, B.]]
[[Category: Forstrom, R J.]]
[[Category: Rosnes, I.]]
[[Category: Rowe, A D.]]
[[Category: Hydrolase]]

Revision as of 20:22, 17 April 2013

Template:STRUCTURE 4b20

Structural basis of DNA loop recognition by Endonuclease V

Template:ABSTRACT PUBMED 23313664

Function

[NFI_THEMA] Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA. Acts in DNA repair. In vitro, can also cleave single-stranded substrates with inosine, double-stranded DNA with apurinic sites, or DNA sites with uracil or a mismatched base. When present in molar excess, two protein molecules can bind to the same DNA substrate and effect cleavage of both strands (in vitro).[1]

About this Structure

4b20 is a 6 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

  1. ↑ Huang J, Lu J, Barany F, Cao W. Mutational analysis of endonuclease V from Thermotoga maritima. Biochemistry. 2002 Jul 2;41(26):8342-50. PMID:12081482

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