1yd4: Difference between revisions

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[[Image:1yd4.png|left|200px]]
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{{STRUCTURE_1yd4|  PDB=1yd4  |  SCENE=  }}  
{{STRUCTURE_1yd4|  PDB=1yd4  |  SCENE=  }}  
===Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Thermotoga maritima: Point mutant Y29F bound to its catalytic divalent cation===
===Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Thermotoga maritima: Point mutant Y29F bound to its catalytic divalent cation===
{{ABSTRACT_PUBMED_15692561}}


==Function==
[[http://www.uniprot.org/uniprot/UVRC_THEMA UVRC_THEMA]] The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision (By similarity).


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==About this Structure==
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[[1yd4]] is a 1 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=1YD4 OCA].
(as it appears on PubMed at http://www.pubmed.gov), where 15692561 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15692561}}


==About this Structure==
==See Also==
1YD4 is a 1 chain structure of 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=1YD4 OCA].
*[[UvrABC|UvrABC]]


==Reference==
==Reference==
<ref group="xtra">PMID:15692561</ref><references group="xtra"/>
<ref group="xtra">PMID:015692561</ref><references group="xtra"/><references/>
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Croteau, D L.]]
[[Category: Croteau, D L.]]
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[[Category: Wang, L.]]
[[Category: Wang, L.]]
[[Category: Dna binding protein]]
[[Category: Dna binding protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 21:14:15 2009''

Revision as of 11:39, 23 April 2014

Template:STRUCTURE 1yd4

Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Thermotoga maritima: Point mutant Y29F bound to its catalytic divalent cationCrystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Thermotoga maritima: Point mutant Y29F bound to its catalytic divalent cation

Template:ABSTRACT PUBMED 15692561

FunctionFunction

[UVRC_THEMA] The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision (By similarity).

About this StructureAbout this Structure

1yd4 is a 1 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

See AlsoSee Also

ReferenceReference

[xtra 1]

  1. ↑ Truglio JJ, Rhau B, Croteau DL, Wang L, Skorvaga M, Karakas E, DellaVecchia MJ, Wang H, Van Houten B, Kisker C. Structural insights into the first incision reaction during nucleotide excision repair. EMBO J. 2005 Mar 9;24(5):885-94. Epub 2005 Feb 3. PMID:15692561

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