4b20

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''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

Contents

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4b20"
Personal tools