Evidence map›Paper›PMID 27596595›Full record

ArticleNucleic acids research2016

The structure of the pleiotropic transcription regulator CodY provides insight into its GTP-sensing mechanism.

Ah-Reum Han, Hye-Ri Kang, Jonghyeon Son, Do Hoon Kwon, Sulhee Kim, Woo Cheol Lee, Hyun Kyu Song, Moon Jung Song, Kwang Yeon Hwang

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

21 citing papers in PubMed, 34 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 1 institution in 1 country.

Ah-Reum HanDepartment of Biosystems & Biotechnology, Korea University, Anam-dong, Seoungbuk-gu, Seoul 136-713, South Korea.
Hye-Ri KangDepartment of Biosystems & Biotechnology, Korea University, Anam-dong, Seoungbuk-gu, Seoul 136-713, South Korea.
Jonghyeon SonDepartment of Biosystems & Biotechnology, Korea University, Anam-dong, Seoungbuk-gu, Seoul 136-713, South Korea.
Do Hoon KwonDepartment of Life Sciences, College of Life Sciences & Biotechnology, Korea University, Anam-dong, Seoungbuk-gu, Seoul 136-713, South Korea.
Sulhee KimDepartment of Biosystems & Biotechnology, Korea University, Anam-dong, Seoungbuk-gu, Seoul 136-713, South Korea.
Woo Cheol LeeDepartment of Biosystems & Biotechnology, Korea University, Anam-dong, Seoungbuk-gu, Seoul 136-713, South Korea.
Hyun Kyu SongDepartment of Life Sciences, College of Life Sciences & Biotechnology, Korea University, Anam-dong, Seoungbuk-gu, Seoul 136-713, South Korea.
Moon Jung SongDepartment of Biosystems & Biotechnology, Korea University, Anam-dong, Seoungbuk-gu, Seoul 136-713, South Korea.ORCID http://orcid.org/0000-0003-3649-6987
Kwang Yeon HwangDepartment of Biosystems & Biotechnology, Korea University, Anam-dong, Seoungbuk-gu, Seoul 136-713, South Korea chahong@korea.ac.kr.
Korea University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

GTP and branched-chain amino acids (BCAAs) are metabolic sensors that are indispensable for the determination of the metabolic status of cells. However, their molecular sensing mechanism remains unclear. CodY is a unique global transcription regulator that recognizes GTP and BCAAs as specific signals and affects expression of more than 100 genes associated with metabolism. Herein, we report the first crystal structures of the full-length CodY complex with sensing molecules and describe their functional states. We observed two different oligomeric states of CodY: a dimeric complex of CodY from Staphylococcus aureus with the two metabolites GTP and isoleucine, and a tetrameric form (apo) of CodY from Bacillus cereus Notably, the tetrameric state shows in an auto-inhibitory manner by blocking the GTP-binding site, whereas the binding sites of GTP and isoleucine are clearly visible in the dimeric state. The GTP is located at a hinge site between the long helical region and the metabolite-binding site. Together, data from structural and electrophoretic mobility shift assay analyses improve understanding of how CodY senses GTP and operates as a DNA-binding protein and a pleiotropic transcription regulator.

Indexed as

Models, MolecularAmino Acid SequenceBacterial ProteinsBinding SitesDNAGuanosine TriphosphateProtein ConformationProtein Interaction Domains and MotifsRepressor ProteinsStructure-Activity RelationshipTranscription FactorsBacterial ProteinsCodY protein, Staphylococcus aureusDNAGuanosine TriphosphateRepressor ProteinsTranscription Factors

Identifiers

PMID27596595
PMCPMC5100569
OpenAlexW2511373692

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.