Evidence map›Paper›PMID 20944208›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010

The structure of the first representative of Pfam family PF09836 reveals a two-domain organization and suggests involvement in transcriptional regulation.

Debanu Das, Nick V Grishin, Abhinav Kumar, Dennis Carlton, Constantina Bakolitsa, Mitchell D Miller, Polat Abdubek, Tamara Astakhova, Herbert L Axelrod, Prasad Burra and 46 more

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

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  7. A mixed-valent Fe(II)Fe(III) species converts cysteine to an oxazolone/thioamide pair in methanobactin biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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

56 authors.

Debanu DasStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA, USA.
Nick V Grishin
Abhinav Kumar
Dennis Carlton
Constantina Bakolitsa
Mitchell D Miller
Polat Abdubek
Tamara Astakhova
Herbert L Axelrod
Prasad Burra
Connie Chen
Hsiu Ju Chiu
Michelle Chiu
Thomas Clayton
Marc C Deller
Lian Duan
Kyle Ellrott
Dustin Ernst
Carol L Farr
Julie Feuerhelm
Anna Grzechnik
Slawomir K Grzechnik
Joanna C Grant
Gye Won Han
Lukasz Jaroszewski
Kevin K Jin
Hope A Johnson
Heath E Klock
Mark W Knuth
Piotr Kozbial
S Sri Krishna
David Marciano
Daniel McMullan
Andrew T Morse
Edward Nigoghossian
Amanda Nopakun
Linda Okach
Silvya Oommachen
Jessica Paulsen
Christina Puckett
Ron Reyes
Christopher L Rife
Natasha Sefcovic
Henry J Tien
Christine B Trame
Henry van den Bedem
Dana Weekes
Tiffany Wooten
Qingping Xu
Keith O Hodgson
John Wooley
Marc André Elsliger
Ashley M Deacon
Adam Godzik
Scott A Lesley
Ian A Wilson

Funding

Technology Evaluation CoreU54GM074898 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI STEVENS, RAYMOND C · 2005 to 2009
$50.6M
NIGMS NIH HHS U54 GM074898
6 · The paper itself

Abstract

Proteins with the DUF2063 domain constitute a new Pfam family, PF09836. The crystal structure of a member of this family, NGO1945 from Neisseria gonorrhoeae, has been determined and reveals that the N-terminal DUF2063 domain is likely to be a DNA-binding domain. In conjunction with the rest of the protein, NGO1945 is likely to be involved in transcriptional regulation, which is consistent with genomic neighborhood analysis. Of the 216 currently known proteins that contain a DUF2063 domain, the most significant sequence homologs of NGO1945 (∼40-99% sequence identity) are from various Neisseria and Haemophilus species. As these are important human pathogens, NGO1945 represents an interesting candidate for further exploration via biochemical studies and possible therapeutic intervention.

Indexed as

Gene Expression RegulationTranscription, GeneticAmino Acid SequenceBacterial ProteinsCrystallography, X-RayGenome, BacterialModels, MolecularMolecular Sequence DataNeisseria gonorrhoeaeProtein Structure, QuaternaryProtein Structure, TertiaryStructural Homology, ProteinBacterial Proteins

Identifiers

PMID20944208
PMCPMC2954202

What OpenQuestion holds

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LicenceCC BY
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.