Evidence map›Paper›PMID 28374778›Full record

ArticleScientific reports2017

Structural basis for a novel type of cytokinin-activating protein.

Hogyun Seo, Kyung-Jin Kim

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.0field-weighted citation impact, top 10% 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

14 citing papers in PubMed, 30 citations in OpenAlex.

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  8. The structure of the Moco carrier protein from Rippkaea orientalis.Acta crystallographica. Section F, Structural biology communications · 2020
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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

2 authors at 1 institution in 1 country.

Hogyun SeoSchool of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University, Daegu 702-701, Republic of Korea.
Kyung-Jin KimSchool of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University, Daegu 702-701, Republic of Korea.
Kyungpook National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Lonely Guy (LOG) protein has been identified as a crucial enzyme involved in the production of cytokinins, which are important phytohormones, in plants and plant-interacting organisms. However, C. glutamicum has an isoform (Cg1261) of LOG that contains an extended N-terminal region compared to those of known LOGs, and this type of isoforms are also found in a variety of organisms. Nevertheless, these proteins are considered as lysine decarboxylases, without their functional characterization. To investigate the function of Cg1261, we determined its crystal structure at a resolution of 1.95 Å. Unlike known dimeric LOGs, Cg1261 was found to form a hexamer. The overall shape of the hexamer resembles a trillium flower, in which a twisted dimer constitutes each petal. The dimeric petal is well superposed with known LOG dimers, and its active site conformation is similar to those of LOG dimers, suggesting that the hexameric LOG-like protein also acts as a LOG. Biochemical and in vivo cytokinin production studies on Cg1261 confirms that Cg1261 functions as a cytokinin-activating protein. Phylogenetic tree analysis using 123 LOG-like proteins suggest that the LOG-like proteins can be categorized to the dimeric type-I LOG and the hexameric type-II LOG.

Indexed as

Amino Acid SequenceBacterial ProteinsCatalytic DomainCorynebacterium glutamicumCrystallography, X-RayCytokininsModels, MolecularPhylogenyProtein MultimerizationStructural Homology, ProteinStructure-Activity RelationshipBacterial ProteinsCytokinins

Identifiers

PMID28374778
PMCPMC5379747
OpenAlexW2605149494

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Registered trials

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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.