Evidence map›Paper›PMID 26464437›Full record

ArticleNucleic acids research2015

Crystallographic characterization of the ribosomal binding site and molecular mechanism of action of Hygromycin A.

Tatsuya Kaminishi, Andreas Schedlbauer, Attilio Fabbretti, Letizia Brandi, Borja Ochoa-Lizarralde, Cheng-Guang He, Pohl Milón, Sean R Connell, Claudio O Gualerzi, Paola Fucini

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.3field-weighted citation impact, top 38% 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

10 citing papers in PubMed, 21 citations in OpenAlex.

  1. ABeilstein journal of organic chemistry · 2024
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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

10 authors at 4 institutions in 3 countries.

Tatsuya KaminishiStructural Biology Unit, CIC bioGUNE, Parque Tecnológico de Bizkaia, 48160 Derio, Bizkaia, Spain.ORCID http://orcid.org/0000-0001-5056-1074
Andreas SchedlbauerStructural Biology Unit, CIC bioGUNE, Parque Tecnológico de Bizkaia, 48160 Derio, Bizkaia, Spain.
Attilio FabbrettiLaboratory of Genetics, Department of Biosciences and Veterinary Medicine, University of Camerino, 62032 Camerino, Italy.
Letizia BrandiLaboratory of Genetics, Department of Biosciences and Veterinary Medicine, University of Camerino, 62032 Camerino, Italy.
Borja Ochoa-LizarraldeStructural Biology Unit, CIC bioGUNE, Parque Tecnológico de Bizkaia, 48160 Derio, Bizkaia, Spain.
Cheng-Guang HeLaboratory of Genetics, Department of Biosciences and Veterinary Medicine, University of Camerino, 62032 Camerino, Italy.
Pohl MilónSchool of Medicine, Faculty of Health Sciences, Universidad Peruana de Ciencias Aplicadas - UPC, Lima, L-33, Perú
Sean R ConnellStructural Biology Unit, CIC bioGUNE, Parque Tecnológico de Bizkaia, 48160 Derio, Bizkaia, Spain IKERBASQUE, Basque Foundation for Science, 48013 Bilbao, Spain sean.connell@gmail.com.ORCID http://orcid.org/0000-0001-7807-7049
Claudio O GualerziLaboratory of Genetics, Department of Biosciences and Veterinary Medicine, University of Camerino, 62032 Camerino, Italy claudio.gualerzi@unicam.it.
Paola FuciniStructural Biology Unit, CIC bioGUNE, Parque Tecnológico de Bizkaia, 48160 Derio, Bizkaia, Spain IKERBASQUE, Basque Foundation for Science, 48013 Bilbao, Spain pfucini@gmail.com.ORCID http://orcid.org/0000-0003-1724-8507
Università di Camerino · ITCIC bioGUNE · ESIkerbasque · ESPeruvian University of Applied Sciences · PE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hygromycin A (HygA) binds to the large ribosomal subunit and inhibits its peptidyl transferase (PT) activity. The presented structural and biochemical data indicate that HygA does not interfere with the initial binding of aminoacyl-tRNA to the A site, but prevents its subsequent adjustment such that it fails to act as a substrate in the PT reaction. Structurally we demonstrate that HygA binds within the peptidyl transferase center (PTC) and induces a unique conformation. Specifically in its ribosomal binding site HygA would overlap and clash with aminoacyl-A76 ribose moiety and, therefore, its primary mode of action involves sterically restricting access of the incoming aminoacyl-tRNA to the PTC.

Indexed as

Binding SitesCinnamatesCrystallography, X-RayHygromycin BModels, MolecularPeptidyl TransferasesProtein Synthesis InhibitorsRibosome Subunits, Large, BacterialRNA, Transfer, Amino AcylCinnamateshygromycin AHygromycin BPeptidyl TransferasesProtein Synthesis InhibitorsRNA, Transfer, Amino Acyl

Identifiers

PMID26464437
PMCPMC4787777
OpenAlexW2096333440

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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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.