1c4o
From Proteopedia
(New page: 200px<br /><applet load="1c4o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c4o, resolution 1.50Å" /> '''CRYSTAL STRUCTURE OF...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1c4o.gif|left|200px]]<br /><applet load="1c4o" size=" | + | [[Image:1c4o.gif|left|200px]]<br /><applet load="1c4o" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1c4o, resolution 1.50Å" /> | caption="1c4o, resolution 1.50Å" /> | ||
'''CRYSTAL STRUCTURE OF THE DNA NUCLEOTIDE EXCISION REPAIR ENZYME UVRB FROM THERMUS THERMOPHILUS'''<br /> | '''CRYSTAL STRUCTURE OF THE DNA NUCLEOTIDE EXCISION REPAIR ENZYME UVRB FROM THERMUS THERMOPHILUS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Nucleotide excision repair (NER) is the most important DNA-repair | + | Nucleotide excision repair (NER) is the most important DNA-repair mechanism in living organisms. In prokaryotes, three enzymes forming the UvrABC system initiate NER of a variety of structurally different DNA lesions. UvrB, the central component of this system, is responsible for the ultimate DNA damage recognition and participates in the incision of the damaged DNA strand. The crystal structure of Thermus thermophilus UvrB reveals a core that is structurally similar to core regions found in helicases, where they constitute molecular motors. Additional domains implicated in binding to DNA and various components of the NER system are attached to this central core. The architecture and distribution of DNA binding sites suggest a possible model for the DNA damage recognition process. |
==About this Structure== | ==About this Structure== | ||
| - | 1C4O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with BOG and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1C4O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=BOG:'>BOG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4O OCA]. |
==Reference== | ==Reference== | ||
| Line 24: | Line 24: | ||
[[Category: uvrabc]] | [[Category: uvrabc]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:02:19 2008'' |
Revision as of 10:02, 21 February 2008
|
CRYSTAL STRUCTURE OF THE DNA NUCLEOTIDE EXCISION REPAIR ENZYME UVRB FROM THERMUS THERMOPHILUS
Overview
Nucleotide excision repair (NER) is the most important DNA-repair mechanism in living organisms. In prokaryotes, three enzymes forming the UvrABC system initiate NER of a variety of structurally different DNA lesions. UvrB, the central component of this system, is responsible for the ultimate DNA damage recognition and participates in the incision of the damaged DNA strand. The crystal structure of Thermus thermophilus UvrB reveals a core that is structurally similar to core regions found in helicases, where they constitute molecular motors. Additional domains implicated in binding to DNA and various components of the NER system are attached to this central core. The architecture and distribution of DNA binding sites suggest a possible model for the DNA damage recognition process.
About this Structure
1C4O is a Single protein structure of sequence from Thermus thermophilus with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the DNA nucleotide excision repair enzyme UvrB from Thermus thermophilus., Machius M, Henry L, Palnitkar M, Deisenhofer J, Proc Natl Acad Sci U S A. 1999 Oct 12;96(21):11717-22. PMID:10518516
Page seeded by OCA on Thu Feb 21 12:02:19 2008
