Evidence map›Paper›PMID 25995122›Full record

ArticleScientific reports2015

Bioinformatical analysis of the sequences, structures and functions of fungal polyketide synthase product template domains.

Lu Liu, Zheng Zhang, Chang-Lun Shao, Jin-Lan Wang, Hong Bai, Chang-Yun Wang

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.4field-weighted citation impact, top 9% 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

28 citing papers in PubMed, 50 citations in OpenAlex.

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  7. Review
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  11. Article
  12. High Diversity of Type I Polyketide Genes inJournal of fungi (Basel, Switzerland) · 2022
    Article
  13. Core Steps to the Azaphilone Family of Fungal Natural Products.Chembiochem : a European journal of chemical biology · 2021
    Review
  14. Article
  15. Article
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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

6 authors at 3 institutions in 1 country.

Lu LiuKey Laboratory of Marine Drugs, the Ministry of Education of China, School of Medicine and Pharmacy, Ocean University of China, Qingdao 266003, China.
Zheng ZhangState Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, China.
Chang-Lun ShaoKey Laboratory of Marine Drugs, the Ministry of Education of China, School of Medicine and Pharmacy, Ocean University of China, Qingdao 266003, China.
Jin-Lan WangSchool of Life Science, Shandong University, Jinan 250100, China.
Hong BaiKey Laboratory of Marine Drugs, the Ministry of Education of China, School of Medicine and Pharmacy, Ocean University of China, Qingdao 266003, China.
Chang-Yun Wang1] Key Laboratory of Marine Drugs, the Ministry of Education of China, School of Medicine and Pharmacy, Ocean University of China, Qingdao 266003, China [2] Institute of Evolution &Marine Biodiversity, Ocean University of China, Qingdao 266003, China.
Ocean University of China · CNShandong University · CNState Key Laboratory of Microbial Technology

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The product template (PT) domains, specifically in fungal non-reducing polyketide synthases (NR-PKSs), mediate the regioselective cyclization of polyketides dominating the final structures. However, up to date, the systematic knowledge about PT domains has been insufficient. In present study, the relationships between sequences, structures and functions of the PT domains were analyzed with 661 NR-PKS sequences. Based on the phylogenetic analysis, the PT domains were classified into prominent eight groups (I-VIII) corresponding with the representative compounds and cyclization regioselectivity (C2-C7, C4-C9, and C6-C11). Most of the cavity lining residue (CLR) sites in all groups were common, while the regional CLR site mutations resulted in the appearance of finger-like regions with different orientation. The cavity volumes and shapes, even the catalytic dyad positions of PT domains in different groups were corresponding with characteristic cyclization regioselectivity and compound sizes. The conservative residues in PT sequences were responsible for the cyclization functions and the evolution of the key residues resulted in the differentiations of cyclization functions. The above findings may help to better understand the cyclization mechanisms of PT domains and even predict the structural types of the aromatic polyketide products.

Indexed as

Computational BiologyAspergillusColletotrichumCrystallography, X-RayDatabases, GeneticFungal ProteinsMolecular Dynamics SimulationPhylogenyPolyketide SynthasesProtein Structure, TertiaryTalaromycesFungal ProteinsPolyketide Synthases

Identifiers

PMID25995122
PMCPMC5386248
OpenAlexW328792416

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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.