Evidence map›Paper›PMID 29095151›Full record

ArticleActa crystallographica. Section F, Structural biology communications2017

The N253F mutant structure of trehalose synthase from Deinococcus radiodurans reveals an open active-site topology.

Sih Yao Chow, Yung Lin Wang, Yu Chiao Hsieh, Guan Chiun Lee, Shwu Huey Liaw

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 87% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. Structural and Mutational Analyses of Trehalose Synthase fromJournal of agricultural and food chemistry · 2024
    Article
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

5 authors at 2 institutions in 1 country.

Sih Yao ChowDepartment of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, No. 155, Sec. 2, Linong Street, Taipei 11221, Taiwan.
Yung Lin WangDepartment of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, No. 155, Sec. 2, Linong Street, Taipei 11221, Taiwan.
Yu Chiao HsiehDepartment of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, No. 155, Sec. 2, Linong Street, Taipei 11221, Taiwan.
Guan Chiun LeeDepartment of Life Science, National Taiwan Normal University, No. 162, Sec. 1, Heping East Road, Taipei 11677, Taiwan.
Shwu Huey LiawDepartment of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, No. 155, Sec. 2, Linong Street, Taipei 11221, Taiwan.
National Yang Ming Chiao Tung University · TWNational Taiwan Normal University · TW

Funding

Ministry of Science and Technology, Taiwan MOST 105-2311-B-010-001
6 · The paper itself

Abstract

Trehalose synthase (TS) catalyzes the reversible conversion of maltose to trehalose and belongs to glycoside hydrolase family 13 (GH13). Previous mechanistic analysis suggested a rate-limiting protein conformational change, which is probably the opening and closing of the active site. Consistently, crystal structures of Deinococcus radiodurans TS (DrTS) in complex with the inhibitor Tris displayed an enclosed active site for catalysis of the intramoleular isomerization. In this study, the apo structure of the DrTS N253F mutant displays a new open conformation with an empty active site. Analysis of these structures suggests that substrate binding induces a domain rotation to close the active site. Such a substrate-induced domain rotation has also been observed in some other GH13 enzymes.

Indexed as

MutationCatalytic DomainCrystallography, X-RayDeinococcusGlucosyltransferasesModels, MolecularProtein ConformationSubstrate SpecificityGlucosyltransferasestrehalose synthaseconformational changedomain rotationenzyme mechanismglycoside hydrolase family 13trehalose synthaseX-ray crystallography

Identifiers

PMID29095151
PMCPMC5683027
OpenAlexW2765939284

What OpenQuestion holds

Textmetadata
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.