6ZQP

Structure of the Pmt2-MIR domain with bound ligands

6ZQP の概要

• エントリーDOI: 10.2210/pdb6zqp/pdb
• 分子名称: PMT2 isoform 1, TETRAETHYLENE GLYCOL, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: carbohydrate-binding module, mir domain, protein-o-mannosylation, beta-trefoil, peptide binding protein
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25584.24

構造登録者

Wild, K.,Chiapparino, A.,Hackmann, Y.,Mortensen, S.,Sinning, I. (登録日: 2020-07-10, 公開日: 2020-12-23, 最終更新日: 2024-10-23)

主引用文献

Chiapparino, A.,Grbavac, A.,Jonker, H.R.,Hackmann, Y.,Mortensen, S.,Zatorska, E.,Schott, A.,Stier, G.,Saxena, K.,Wild, K.,Schwalbe, H.,Strahl, S.,Sinning, I.
Functional implications of MIR domains in protein O -mannosylation.
Elife, 9:-, 2020

PubMed Abstract: Protein -mannosyltransferases (PMTs) represent a conserved family of multispanning endoplasmic reticulum membrane proteins involved in glycosylation of S/T-rich protein substrates and unfolded proteins. PMTs work as dimers and contain a luminal MIR domain with a β-trefoil fold, which is susceptive for missense mutations causing α-dystroglycanopathies in humans. Here, we analyze PMT-MIR domains by an integrated structural biology approach using X-ray crystallography and NMR spectroscopy and evaluate their role in PMT function in vivo. We determine Pmt2- and Pmt3-MIR domain structures and identify two conserved mannose-binding sites, which are consistent with general β-trefoil carbohydrate-binding sites (α, β), and also a unique PMT2-subfamily exposed FKR motif. We show that conserved residues in site α influence enzyme processivity of the Pmt1-Pmt2 heterodimer in vivo. Integration of the data into the context of a Pmt1-Pmt2 structure and comparison with homologous β-trefoil - carbohydrate complexes allows for a functional description of MIR domains in protein -mannosylation.

PubMed: 33357379
DOI: 10.7554/eLife.61189

実験手法

X-RAY DIFFRACTION (1.6 Å)