Evidence map›Paper›PMID 25084374›Full record

ArticleActa crystallographica. Section F, Structural biology communications2014

The RpfC (Rv1884) atomic structure shows high structural conservation within the resuscitation-promoting factor catalytic domain.

Francois Xavier Chauviac, Giles Robertson, Doris H X Quay, Claire Bagnéris, Christian Dumas, Brian Henderson, John Ward, Nicholas H Keep, Martin Cohen-Gonsaud

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

11 citing papers in PubMed, 16 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

9 authors at 5 institutions in 2 countries.

Francois Xavier ChauviacCrystallography, Institute for Structural and Molecular Biology, Department of Biological Sciences, Birkbeck, University of London, Malet Street, London WC1E 7HX, England.
Giles RobertsonCrystallography, Institute for Structural and Molecular Biology, Department of Biological Sciences, Birkbeck, University of London, Malet Street, London WC1E 7HX, England.
Doris H X QuayCrystallography, Institute for Structural and Molecular Biology, Department of Biological Sciences, Birkbeck, University of London, Malet Street, London WC1E 7HX, England.
Claire BagnérisCrystallography, Institute for Structural and Molecular Biology, Department of Biological Sciences, Birkbeck, University of London, Malet Street, London WC1E 7HX, England.
Christian DumasCentre de Biochimie Structurale, CNRS UMR 5048, 29 Rue de Navacelles, 34090 Montpellier, France; INSERM U1054, Université Montpellier I, Montpellier, France.
Brian HendersonDepartment of Microbial Diseases, UCL-Eastman Dental Institute, University College London, 256 Gray's Inn Road, London WC1X 8LD, England.
John WardThe Advanced Centre for Biochemical Engineering, Department of Biochemical Engineering, University College London, Torrington Place, London WC1E 7JE, England.
Nicholas H KeepCrystallography, Institute for Structural and Molecular Biology, Department of Biological Sciences, Birkbeck, University of London, Malet Street, London WC1E 7HX, England.
Martin Cohen-GonsaudCrystallography, Institute for Structural and Molecular Biology, Department of Biological Sciences, Birkbeck, University of London, Malet Street, London WC1E 7HX, England.
Birkbeck, University of London · GBBiochemical Society · GBCentre de Biologie Structurale · FRInserm · FRUniversity College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F011148/1Medical Research Council G0401038
6 · The paper itself

Abstract

The first structure of the catalytic domain of RpfC (Rv1884), one of the resuscitation-promoting factors (RPFs) from Mycobacterium tuberculosis, is reported. The structure was solved using molecular replacement once the space group had been correctly identified as twinned P21 rather than the apparent C2221 by searching for anomalous scattering sites in P1. The structure displays a very high degree of structural conservation with the previously published structures of the catalytic domains of RpfB (Rv1009) and RpfE (Rv2450). This structural conservation highlights the importance of the versatile domain composition of the RPF family.

Indexed as

Amino Acid SequenceBacterial ProteinsCatalytic DomainModels, MolecularMolecular Sequence DataMycobacterium tuberculosisProtein ConformationSequence Homology, Amino AcidBacterial ProteinsMycobacterium tuberculosispeptidoglycanresuscitation-promoting factor

Identifiers

PMID25084374
PMCPMC4118796
OpenAlexW1980375781

What OpenQuestion holds

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LicenceCC BY
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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.