2j6v: Difference between revisions

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==Overview==
==Overview==
The ultraviolet damage endonuclease (UVDE) performs the initial step in an, alternative excision repair pathway of UV-induced DNA damage, nicking, immediately adjacent to the 5' phosphate of the damaged nucleotides., Unique for a single-protein DNA repair endonuclease, it can detect, different types of damage. Here we show that Thermus thermophilus UVDE, shares some essential structural features with Endo IV, an enzyme from the, base excision repair pathway that exclusively nicks at abasic sites. A, comparison between the structures indicates how DNA is bound by UVDE, how, UVDE may recognize damage, and which of its residues are involved in, catalysis. Furthermore, the comparison suggests an elegant explanation of, UVDE's potential to recognize different types of damage. Incision assays, including point mutants of UVDE confirmed the relevance of these, conclusions.
The ultraviolet damage endonuclease (UVDE) performs the initial step in an alternative excision repair pathway of UV-induced DNA damage, nicking immediately adjacent to the 5' phosphate of the damaged nucleotides. Unique for a single-protein DNA repair endonuclease, it can detect different types of damage. Here we show that Thermus thermophilus UVDE shares some essential structural features with Endo IV, an enzyme from the base excision repair pathway that exclusively nicks at abasic sites. A comparison between the structures indicates how DNA is bound by UVDE, how UVDE may recognize damage, and which of its residues are involved in catalysis. Furthermore, the comparison suggests an elegant explanation of UVDE's potential to recognize different types of damage. Incision assays including point mutants of UVDE confirmed the relevance of these conclusions.


==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: Abrahams, J.P.]]
[[Category: Abrahams, J P.]]
[[Category: Goossen, N.]]
[[Category: Goossen, N.]]
[[Category: Pannu, N.S.]]
[[Category: Pannu, N S.]]
[[Category: Paspaleva, K.]]
[[Category: Paspaleva, K.]]
[[Category: Thomassen, E.A.J.]]
[[Category: Thomassen, E A.J.]]
[[Category: MN]]
[[Category: MN]]
[[Category: PO4]]
[[Category: PO4]]
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[[Category: uvde]]
[[Category: uvde]]


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Revision as of 18:59, 21 February 2008

File:2j6v.gif


2j6v, resolution 1.55Å

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CRYSTAL STRUCTURE OF THE DNA REPAIR ENZYME UV DAMAGE ENDONUC

OverviewOverview

The ultraviolet damage endonuclease (UVDE) performs the initial step in an alternative excision repair pathway of UV-induced DNA damage, nicking immediately adjacent to the 5' phosphate of the damaged nucleotides. Unique for a single-protein DNA repair endonuclease, it can detect different types of damage. Here we show that Thermus thermophilus UVDE shares some essential structural features with Endo IV, an enzyme from the base excision repair pathway that exclusively nicks at abasic sites. A comparison between the structures indicates how DNA is bound by UVDE, how UVDE may recognize damage, and which of its residues are involved in catalysis. Furthermore, the comparison suggests an elegant explanation of UVDE's potential to recognize different types of damage. Incision assays including point mutants of UVDE confirmed the relevance of these conclusions.

About this StructureAbout this Structure

2J6V is a Single protein structure of sequence from Thermus thermophilus with and as ligands. Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the DNA repair enzyme ultraviolet damage endonuclease., Paspaleva K, Thomassen E, Pannu NS, Iwai S, Moolenaar GF, Goosen N, Abrahams JP, Structure. 2007 Oct;15(10):1316-24. PMID:17937920

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