1c4o: Difference between revisions

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|PDB= 1c4o |SIZE=350|CAPTION= <scene name='initialview01'>1c4o</scene>, resolution 1.50&Aring;
|PDB= 1c4o |SIZE=350|CAPTION= <scene name='initialview01'>1c4o</scene>, resolution 1.50&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
|LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c4o OCA], [http://www.ebi.ac.uk/pdbsum/1c4o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c4o RCSB]</span>
}}
}}


Line 26: Line 29:
[[Category: Machius, M.]]
[[Category: Machius, M.]]
[[Category: Palnitkar, M.]]
[[Category: Palnitkar, M.]]
[[Category: BOG]]
[[Category: SO4]]
[[Category: dna nucleotide excision repair]]
[[Category: dna nucleotide excision repair]]
[[Category: helicase]]
[[Category: helicase]]
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[[Category: uvrabc]]
[[Category: uvrabc]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:19:43 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:14:25 2008''

Revision as of 16:14, 30 March 2008

File:1c4o.gif


Drag the structure with the mouse to rotate
1c4o, resolution 1.50Å
Ligands: BOG, SO4
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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

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