Evidence map›Paper›PMID 21923197›Full record

ArticleBiochemistry2011

Structural insights into complete metal ion coordination from ternary complexes of B family RB69 DNA polymerase.

Shuangluo Xia, Mina Wang, Gregor Blaha, William H Konigsberg, Jimin Wang

Abstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

28 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Innovative nucleic acid detection ofFrontiers in cellular and infection microbiology · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Crystallographic evidence for two-metal-ion catalysis in human pol η.Protein science : a publication of the Protein Society · 2019
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Shuangluo XiaDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 96520-8114, United States.
Mina Wang
Gregor Blaha
William H Konigsberg
Jimin Wang

Funding

Molecular Biology and Structure of a DNA ReplicaseR01GM063276 · NIGMS · YALE UNIVERSITY · PI KONIGSBERG, WILLIAM H · 2001 to 2013
$4.2M
NIGMS NIH HHS 3R01GM063276-08S1NIGMS NIH HHS R01 GM063276NIGMS NIH HHS R01 GM063276-9
6 · The paper itself

Abstract

We have captured a preinsertion ternary complex of RB69 DNA polymerase (RB69pol) containing the 3' hydroxyl group at the terminus of an extendable primer (ptO3') and a nonhydrolyzable 2'-deoxyuridine 5'-α,β-substituted triphosphate, dUpXpp, where X is either NH or CH(2), opposite a complementary templating dA nucleotide residue. Here we report four structures of these complexes formed by three different RB69pol variants with catalytically inert Ca(2+) and four other structures with catalytically competent Mn(2+) or Mg(2+). These structures provide new insights into why the complete divalent metal-ion coordination complexes at the A and B sites are required for nucleotidyl transfer. They show that the metal ion in the A site brings ptO3' close to the α-phosphorus atom (Pα) of the incoming dNTP to enable phosphodiester bond formation through simultaneous coordination of both ptO3' and the nonbridging Sp oxygen of the dNTP's α-phosphate. The coordination bond length of metal ion A as well as its ionic radius determines how close ptO3' can approach Pα. These variables are expected to affect the rate of bond formation. The metal ion in the B site brings the pyrophosphate product close enough to Pα to enable pyrophosphorolysis and assist in the departure of the pyrophosphate. In these dUpXpp-containing complexes, ptO3' occupies the vertex of a distorted metal ion A coordination octahedron. When ptO3' is placed at the vertex of an undistorted, idealized metal ion A octahedron, it is within bond formation distance to Pα. This geometric relationship appears to be conserved among DNA polymerases of known structure.

Indexed as

Amino Acid SubstitutionCalciumCrystallography, X-RayDiphosphatesDNA-Directed DNA PolymeraseHydrogen BondingMagnesiumManganeseNucleic Acid ConformationNucleic Acid HeteroduplexesPhosphorusViral Proteinsbacteriophage RB69 DNA polymeraseCalciumDiphosphatesDNA-Directed DNA PolymeraseMagnesiumManganeseNucleic Acid HeteroduplexesPhosphorusViral Proteins

Identifiers

PMID21923197
PMCPMC3760225

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.