Evidence map›Paper›PMID 27555514›Full record

ArticleScientific reports2016

A mutagenic study identifying critical residues for the structure and function of rice manganese transporter OsMTP8.1.

Xi Chen, Jiyu Li, Lihua Wang, Gang Ma, Wei Zhang

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

13 citing papers in PubMed.

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  8. Genome-Wide Identification of Metal Tolerance Protein Genes inInternational journal of molecular sciences · 2020
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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

5 authors.

Xi ChenDepartment of Biochemistry &Molecular Biology, College of Life Sciences, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China.
Jiyu LiDepartment of Biochemistry &Molecular Biology, College of Life Sciences, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China.
Lihua WangDepartment of Biochemistry &Molecular Biology, College of Life Sciences, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China.
Gang MaDepartment of Biochemistry &Molecular Biology, College of Life Sciences, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China.
Wei ZhangDepartment of Biochemistry &Molecular Biology, College of Life Sciences, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rice (Oryza sativa) MTP8.1 (OsMTP8.1) is a tonoplast-localized manganese transporter of the cation diffusion facilitator family. Here we present a structure-function analysis of OsMTP8.1 based on the site-directed and random mutagenesis and complementation assays in manganese hypersensitive yeast, in combination with three-dimensional (3D) structure modeling based on the crystal structure of the Escherichia coli CDF family member, EcYiiP. Two metal-binding sites are conserved in OsMTP8.1 with EcYiiP, one is between transmembrane helices TM2 and TM5, the other is the cytoplasmic C-terminus. In addition to these two metal-binding sites, there may exist other Mn-binding sites such as that at the very end of the CTD. Two residues (R167 and L296) may play an important role for the hinge-like movement of CTDs. Several mutations such as E357A and V374D may affect dimer formation, and S132A may induce a conformational change, resulting in a loss of transport function or modification in metal selectivity. The N-terminus of OsMTP8.1 was not functional for Mn transport activity, and the real function of NTD remains to be investigated in the future. The findings of the present study illustrate the structure-function relationship of OsMTP8.1 in Mn transport activity, which may also be applied to other plant Mn-CDF proteins.

Indexed as

Binding SitesCation Transport ProteinsEscherichia coliManganeseModels, MolecularMutagenesis, Site-DirectedOryzaPlant ProteinsProtein ConformationProtein DomainsProtoplastsRecombinant ProteinsSaccharomyces cerevisiaeStructure-Activity RelationshipZincCation Transport ProteinsManganesePlant ProteinsRecombinant ProteinsZinc

Identifiers

PMID27555514
PMCPMC4995437

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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.