ArticleNature structural & molecular biology2019
Structure of the eukaryotic protein O-mannosyltransferase Pmt1-Pmt2 complex.
Article in Nature structural & molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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.
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.
Who cites it
31 citing papers in PubMed, 31 citations in OpenAlex.
- Genome-Guided Discovery of Antimalarial 4-Amino-2,4-Pentadienoate-Containing Cyclolipodepsipeptides.Angewandte Chemie (International ed. in English) · 2026Article
- Recent advances in the synthesis of α-dystroglycanRSC advances · 2026Review
- O-mannosylation of misfolded ER proteins promotes ERAD.The EMBO journal · 2026Article
- Structural characterisation of the fungal Pmt4 homodimer.Nature communications · 2025Article
- Pmt4 recognizes two separate acceptor sites to O-mannosylate in the S/T-rich regions of substrate proteins.Nature communications · 2025Article
- Structural Insights into the Protein Mannosyltransferase from Mycobacterium tuberculosis reveal a WW-Domain-Like Protein Motif in Bacteria.Communications biology · 2025Article
- Structural insights into polyisoprenyl-binding glycosyltransferases.Structure (London, England : 1993) · 2025Review
- Malformations of Core M3 on α-Dystroglycan Are the Leading Cause of Dystroglycanopathies.Journal of molecular neuroscience : MN · 2025Review
- Structural glycobiology - from enzymes to organelles.Biochemical Society transactions · 2025Review
- Differential substrate preferences IN ACTINOBACTERIAL protein O-MANNOSYLTRANSFERASES and alteration of protein-O-MANNOSYLATION by choice of secretion pathway.Glycobiology · 2025Article
- Three-component systems represent a common pathway for extracytoplasmic addition of pentofuranose sugars into bacterial glycans.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Removal of pomt1 in zebrafish leads to loss of α-dystroglycan glycosylation and dystroglycanopathy phenotypes.Human molecular genetics · 2024Article
- Protein O-mannosylation: one sugar, several pathways, many functions.Glycobiology · 2023Review
- Structure of the priming arabinosyltransferase AftA required for AG biosynthesis ofProceedings of the National Academy of Sciences of the United States of America · 2023Article
- The SHDRA syndrome-associated geneProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Yeast as a tool for membrane protein production and structure determination.FEMS yeast research · 2022Article
- Role of Protein Glycosylation in Interactions of Medically Relevant Fungi with the Host.Journal of fungi (Basel, Switzerland) · 2021Review
- Alanine-scanning mutagenesis of protein mannosyl-transferase fromMicrobiology (Reading, England) · 2021Article
- Protein N-glycosylation and O-mannosylation are catalyzed by two evolutionarily related GT-C glycosyltransferases.Current opinion in structural biology · 2021Review
- Structural, Evolutionary, and Functional Analysis of the Protein O-Mannosyltransferase Family in Pathogenic Fungi.Journal of fungi (Basel, Switzerland) · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
In eukaryotes, a nascent peptide entering the endoplasmic reticulum (ER) is scanned by two Sec61 translocon-associated large membrane machines for protein N-glycosylation and protein O-mannosylation, respectively. While the structure of the eight-protein oligosaccharyltransferase complex has been determined recently, the structures of mannosyltransferases of the PMT family, which are an integral part of ER protein homeostasis, are still unknown. Here we report cryo-EM structures of the Saccharomyces cerevisiae Pmt1-Pmt2 complex bound to a donor and an acceptor peptide at 3.2-Å resolution, showing that each subunit contains 11 transmembrane helices and a lumenal β-trefoil fold termed the MIR domain. The structures reveal the substrate recognition model and confirm an inverting mannosyl-transferring reaction mechanism by the enzyme complex. Furthermore, we found that the transmembrane domains of Pmt1 and Pmt2 share a structural fold with the catalytic subunits of oligosaccharyltransferases, confirming a previously proposed evolutionary relationship between protein O-mannosylation and protein N-glycosylation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.