1C4O

CRYSTAL STRUCTURE OF THE DNA NUCLEOTIDE EXCISION REPAIR ENZYME UVRB FROM THERMUS THERMOPHILUS

Summary for 1C4O

• Entry DOI: 10.2210/pdb1c4o/pdb
• Descriptor: DNA NUCLEOTIDE EXCISION REPAIR ENZYME UVRB, octyl beta-D-glucopyranoside, SULFATE ION, ... (4 entities in total)
• Functional Keywords: dna nucleotide excision repair, uvrabc, helicase, hyperthermostable protein, replication
• Biological source: Thermus thermophilus
• Cellular location: Cytoplasm: Q56243
• Total number of polymer chains: 1
• Total formula weight: 77103.91

Authors

Machius, M.,Henry, L.,Palnitkar, M.,Deisenhofer, J. (deposition date: 1999-09-14, release date: 2000-07-26, Last modification date: 2023-12-27)

Primary citation

Machius, M.,Henry, L.,Palnitkar, M.,Deisenhofer, J.
Crystal structure of the DNA nucleotide excision repair enzyme UvrB from Thermus thermophilus.
Proc.Natl.Acad.Sci.USA, 96:11717-11722, 1999

PubMed Abstract: 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.

PubMed: 10518516
DOI: 10.1073/pnas.96.21.11717

Experimental method

X-RAY DIFFRACTION (1.5 Å)