Evidence map›Paper›PMID 29500373›Full record

ArticleScientific reports2018

Structure based function-annotation of hypothetical protein MGG_01005 from Magnaporthe oryzae reveals it is the dynein light chain orthologue of dynlt1/3.

Guorui Li, Jinguang Huang, Jun Yang, Dan He, Chao Wang, Xiaoxuan Qi, Ian A Taylor, Junfeng Liu, You-Liang Peng

Abstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

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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

5 citing papers in PubMed.

  1. Functional domain annotation by structural similarity.NAR genomics and bioinformatics · 2024
    Article
  2. Structural and functional characterization ofFrontiers in microbiology · 2024
    Article
  3. Article
  4. Article
  5. Force-Generating Mechanism of Axonemal Dynein in Solo and Ensemble.International journal of molecular sciences · 2020
    Review
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.

Guorui LiMOA Key Laboratory of Plant Pathology, China Agricultural University, No2 Yunamingyuanxilu, Beijing, 100193, China.
Jinguang HuangMOA Key Laboratory of Plant Pathology, China Agricultural University, No2 Yunamingyuanxilu, Beijing, 100193, China.
Jun YangMOA Key Laboratory of Plant Pathology, China Agricultural University, No2 Yunamingyuanxilu, Beijing, 100193, China.ORCID 0000-0001-6085-9245
Dan HeMOA Key Laboratory of Plant Pathology, China Agricultural University, No2 Yunamingyuanxilu, Beijing, 100193, China.
Chao WangMOA Key Laboratory of Plant Pathology, China Agricultural University, No2 Yunamingyuanxilu, Beijing, 100193, China.
Xiaoxuan QiMOA Key Laboratory of Plant Pathology, China Agricultural University, No2 Yunamingyuanxilu, Beijing, 100193, China.
Ian A TaylorMacromolecular Structure Laboratory, The Francis Crick Institute, London, NW1 1AT, UK. ian.taylor@crick.ac.uk.ORCID 0000-0002-6763-3852
Junfeng LiuMOA Key Laboratory of Plant Pathology, China Agricultural University, No2 Yunamingyuanxilu, Beijing, 100193, China. jliu@cau.edu.cn.
You-Liang PengMOA Key Laboratory of Plant Pathology, China Agricultural University, No2 Yunamingyuanxilu, Beijing, 100193, China. pengyl@cau.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Magnaporthe oryzae is a model fungal plant pathogen employed for studying plant-fungi interactions. Whole genome sequencing and bioinformatics analyses revealed that this fungal pathogen has more than 12,000 protein-coding genes with 65% of the genes remaining functionally un-annotated. Here, we determine the structure of the hypothetical protein, MGG_01005 and show that it is the Magnaporthe oryzae Dynein light chain Tctex-type 1 (dynlt1/3), demonstrated by its structural similarity to other orthologous dynlt1 proteins and its conserved interaction with the N-terminus of the Magnaporthe oryzae dynein intermediate chain, MoDyn1I2. In addition, we present the structure of the MGG_01005-MoDyn1I2 complex together with mutagenesis studies that reveals a di-histidine motif interaction with a glutamate residue in the dynein intermediate chain within a conserved molecular interface. These results demonstrate the utility of structure-based annotation and validate it as a viable approach for the molecular assignment of hypothetic proteins from phyto-pathogenic fungi.

Indexed as

Crystallography, X-RayDyneinsFungal ProteinsMagnaportheProtein ConformationStructure-Activity RelationshipDyneinsFungal Proteins

Identifiers

PMID29500373
PMCPMC5834530

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