1c4o

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1c4o, resolution 1.50Å

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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 BOG and SO4 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

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