1c4o
From Proteopedia
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|PDB= 1c4o |SIZE=350|CAPTION= <scene name='initialview01'>1c4o</scene>, resolution 1.50Å | |PDB= 1c4o |SIZE=350|CAPTION= <scene name='initialview01'>1c4o</scene>, resolution 1.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</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> | ||
}} | }} | ||
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[[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 | + | ''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
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| , resolution 1.50Å | |||||||
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| Ligands: | , | ||||||
| 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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