Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1NK0

ADENINE-GUANINE MISMATCH AT THE POLYMERASE ACTIVE SITE

Summary for 1NK0
Entry DOI10.2210/pdb1nk0/pdb
Related1NJW 1NJX 1NJY 1NJZ 1NK4 1NK5 1NK6 1NK7 1NK8 1NK9 1NKB 1NKC 1NKE
Related PRD IDPRD_900003
DescriptorDNA PRIMER STRAND, DNA TEMPLATE STRAND, DNA POLYMERASE I, ... (7 entities in total)
Functional Keywordsdna polymerase i, dna replication, klenow fragment, protein-dna complex, dna mismatch, transferase-dna complex, transferase/dna
Biological sourceGeobacillus stearothermophilus
Total number of polymer chains3
Total formula weight75062.84
Authors
Johnson, S.J.,Beese, L.S. (deposition date: 2003-01-02, release date: 2004-03-30, Last modification date: 2023-08-16)
Primary citationJohnson, S.J.,Beese, L.S.
Structures of mismatch replication errors observed in a DNA polymerase.
Cell(Cambridge,Mass.), 116:803-816, 2004
Cited by
PubMed Abstract: Accurate DNA replication is essential for genomic stability. One mechanism by which high-fidelity DNA polymerases maintain replication accuracy involves stalling of the polymerase in response to covalent incorporation of mismatched base pairs, thereby favoring subsequent mismatch excision. Some polymerases retain a "short-term memory" of replication errors, responding to mismatches up to four base pairs in from the primer terminus. Here we a present a structural characterization of all 12 possible mismatches captured at the growing primer terminus in the active site of a polymerase. Our observations suggest four mechanisms that lead to mismatch-induced stalling of the polymerase. Furthermore, we have observed the effects of extending a mismatch up to six base pairs from the primer terminus and find that long-range distortions in the DNA transmit the presence of the mismatch back to the enzyme active site, suggesting the structural basis for the short-term memory of replication errors.
PubMed: 15035983
DOI: 10.1016/S0092-8674(04)00252-1
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

226707

数据于2024-10-30公开中

PDB statisticsPDBj update infoContact PDBjnumon