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1NKB

A BACILLUS DNA POLYMERASE I PRODUCT COMPLEX BOUND TO A GUANINE-THYMINE MISMATCH AFTER THREE ROUNDS OF PRIMER EXTENSION, FOLLOWING INCORPORATION OF DCTP, DGTP, AND DTTP.

Summary for 1NKB
Entry DOI10.2210/pdb1nkb/pdb
Related1NJW 1NJX 1NJY 1NJZ 1NK0 1NK4 1NK5 1NK6 1NK7 1NK8 1NK9 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 weight75763.51
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 (2 Å)
Structure validation

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数据于2024-10-30公开中

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