Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication.

Cell (2001), Volume 107, Page 91

Abstract:

Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4) is a DinB homolog that belongs to the recently described Y-family of DNA polymerases, which are best characterized by their low-fidelity synthesis on undamaged DNA templates and propensity to traverse normally replication-blocking lesions. Crystal structures of Dpo4 in ternary complexes with DNA and an incoming nucleotide, either correct or incorrect, have been solved at 1.7 A and 2.1 A resolution, respectively. Despite a conserved active site and a hand-like configuration similar to all known polymerases, Dpo4 makes limited and nonspecific contacts with the replicating base pair, thus relaxing base selection. Dpo4 is also captured in the crystal translocating two template bases to the active site at once, suggesting a possible mechanism for bypassing thymine dimers.

Polymerases:

Topics:

Structure and Structure/Function

Status:

new topics/pols set partial results complete validated

Results:

Polymerase Reference Property Result Context
Dpo4 Ling H2001 Polymerase Catalytic Residue Amino Acids D7, D105, E106
Dpo4 Ling H2001 Cloned or native Cloned in E. coli
Dpo4 Ling H2001 Full length or truncated Full length
Dpo4 Ling H2001 Amino Acids Contacting Template V32, A42, G58
Dpo4 Ling H2001 Amino Acids Contacting NTP G41, A42, A44, A57, G58

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