Evidence map›Paper›PMID 20843803›Full record

ArticleThe Journal of biological chemistry2010

Structure of Escherichia coli AlkA in complex with undamaged DNA.

Brian R Bowman, Seongmin Lee, Shuyu Wang, Gregory L Verdine

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.6field-weighted citation impact, top 18% of its field
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

16 citing papers in PubMed, 23 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Brian R BowmanDepartment of Stem Cell and Regenerative Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
Seongmin Lee
Shuyu Wang
Gregory L Verdine
Harvard University · US

Funding

FUNCTIONALLY TETHERED OLIGONUCLEOTIDESR01GM044853 · NIGMS · HARVARD UNIVERSITY · PI VERDINE, GREGORY LAWRENCE · 1990 to 2011
$5.1M
Structure and Mechanism of Base-Excision DNA RepairR01CA100742 · NCI · HARVARD UNIVERSITY · PI VERDINE, GREGORY LAWRENCE · 2003 to 2013
$3.9M
Structure and Mechanism of the Ire 1 RiboedonucleaseF32GM077935 · NIGMS · HARVARD UNIVERSITY · PI BOWMAN, BRIAN R · 2006 to 2008
$129k
NCI NIH HHS R01 CA100742NIGMS NIH HHS F32 GM077935NIGMS NIH HHS F32 GM077935-01NIGMS NIH HHS GM044853NIGMS NIH HHS R01 GM044853
6 · The paper itself

Abstract

Because DNA damage is so rare, DNA glycosylases interact for the most part with undamaged DNA. Whereas the structural basis for recognition of DNA lesions by glycosylases has been studied extensively, less is known about the nature of the interaction between these proteins and undamaged DNA. Here we report the crystal structures of the DNA glycosylase AlkA in complex with undamaged DNA. The structures revealed a recognition mode in which the DNA is nearly straight, with no amino acid side chains inserted into the duplex, and the target base pair is fully intrahelical. A comparison of the present structures with that of AlkA recognizing an extrahelical lesion revealed conformational changes in both the DNA and protein as the glycosylase transitions from the interrogation of undamaged DNA to catalysis of nucleobase excision. Modeling studies with the cytotoxic lesion 3-methyladenine and accompanying biochemical experiments suggested that AlkA actively interrogates the minor groove of the DNA while probing for the presence of lesions.

Indexed as

AdenineBinding SitesCrystallography, X-RayDNA, BacterialDNA DamageDNA GlycosylasesEscherichia coliEscherichia coli ProteinsHydrogen BondingModels, MolecularMolecular StructureMutationNucleic Acid ConformationProtein BindingProtein Structure, TertiaryTransition Temperature3-methyladenineAdenineDNA-3-methyladenine glycosidase IIDNA, BacterialDNA GlycosylasesEscherichia coli Proteins

Identifiers

PMID20843803
PMCPMC2975202
OpenAlexW2025668322

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.