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

5J2C

Ternary complex crystal structure of DNA polymerase Beta with C:A mismatch at the primer terminus

Summary for 5J2C
Entry DOI10.2210/pdb5j2c/pdb
Related5J0O 5J0P 5J0Q 5J0R 5J0S 5J0T 5J0U 5J0V 5J0W 5J0X 5J0Y 5J29 5J2A 5J2B 5J2D 5J2E 5J2F 5J2G 5J2H 5J2I 5J2J 5J2K
DescriptorDNA polymerase beta, Template Strand, Primer Strand, ... (9 entities in total)
Functional Keywordsdna polymerase beta, mismatch extension, ternary complex, transferase-dna complex, transferase/dna
Biological sourceHomo sapiens (Human)
More
Cellular locationNucleus: P06746
Total number of polymer chains4
Total formula weight48379.43
Authors
Batra, V.K.,Wilson, S.H. (deposition date: 2016-03-29, release date: 2016-10-26, Last modification date: 2024-03-06)
Primary citationBatra, V.K.,Beard, W.A.,Pedersen, L.C.,Wilson, S.H.
Structures of DNA Polymerase Mispaired DNA Termini Transitioning to Pre-catalytic Complexes Support an Induced-Fit Fidelity Mechanism.
Structure, 24:1863-1875, 2016
Cited by
PubMed Abstract: High-fidelity DNA synthesis requires that polymerases display a strong preference for right nucleotide insertion. When the wrong nucleotide is inserted, the polymerase deters extension from the mismatched DNA terminus. Twenty-three crystallographic structures of DNA polymerase β with terminal template-primer mismatches were determined as binary DNA and ternary pre-catalytic substrate complexes. These structures indicate that the mismatched termini adopt various distorted conformations that attempt to satisfy stacking and hydrogen-bonding interactions. The binary complex structures indicate an induced strain in the mismatched template nucleotide. Addition of a non-hydrolyzable incoming nucleotide stabilizes the templating nucleotide with concomitant strain in the primer terminus. Several dead-end ternary complex structures suggest that DNA synthesis might occur as the enzyme transitions from an open to a closed complex. The structures are consistent with an induced-fit mechanism where a mismatched terminus is misaligned relative to the correct incoming nucleotide to deter or delay further DNA synthesis.
PubMed: 27642161
DOI: 10.1016/j.str.2016.08.006
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

227111

건을2024-11-06부터공개중

PDB statisticsPDBj update infoContact PDBjnumon