1JX4

Crystal Structure of a Y-family DNA Polymerase in a Ternary Complex with DNA Substrates and an Incoming Nucleotide

Summary for 1JX4

• Entry DOI: 10.2210/pdb1jx4/pdb
• Related: 1JXL
• Descriptor: 5'-D(*GP*GP*GP*GP*GP*AP*AP*GP*GP*AP*CP*TP*A)-3', 5'-D(*T*TP*CP*AP*TP*TP*AP*GP*TP*CP*CP*TP*TP*CP*CP*CP*CP*C)-3', DNA polymerase IV (family Y), ... (7 entities in total)
• Functional Keywords: dna polymerase, protein-dna complex, y-family, transferase-dna complex, transferase/dna
• Biological source: Sulfolobus solfataricus
• Cellular location: Cytoplasm (Probable): Q97W02
• Total number of polymer chains: 3
• Total formula weight: 50457.98

Authors

Ling, H.,Boudsocq, F.,Woodgate, R.,Yang, W. (deposition date: 2001-09-05, release date: 2001-10-05, Last modification date: 2024-10-16)

Primary citation

Ling, H.,Boudsocq, F.,Woodgate, R.,Yang, W.
Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication.
Cell(Cambridge,Mass.), 107:91-102, 2001

PubMed 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.

PubMed: 11595188
DOI: 10.1016/S0092-8674(01)00515-3

Experimental method

X-RAY DIFFRACTION (1.7 Å)