3RCE

Bacterial oligosaccharyltransferase PglB

3RCE の概要

• エントリーDOI: 10.2210/pdb3rce/pdb
• 分子名称: Oligosaccharide transferase to N-glycosylate proteins, Substrate Mimic Peptide, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: oligosaccharyltransferase, membrane protein, helical bundle, glycosylation, acceptor peptide, plasma membrane, transferase-peptide complex, transferase/peptide
• 由来する生物種: Campylobacter lari; 詳細
• 細胞内の位置: Cell inner membrane ; Multi- pass membrane protein : B9KDD4
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 85314.32

構造登録者

Lizak, C.,Gerber, S.,Numao, S.,Aebi, M.,Locher, K.P. (登録日: 2011-03-31, 公開日: 2011-06-15, 最終更新日: 2025-03-26)

主引用文献

Lizak, C.,Gerber, S.,Numao, S.,Aebi, M.,Locher, K.P.
X-ray structure of a bacterial oligosaccharyltransferase.
Nature, 474:350-355, 2011

PubMed Abstract: Asparagine-linked glycosylation is a post-translational modification of proteins containing the conserved sequence motif Asn-X-Ser/Thr. The attachment of oligosaccharides is implicated in diverse processes such as protein folding and quality control, organism development or host-pathogen interactions. The reaction is catalysed by oligosaccharyltransferase (OST), a membrane protein complex located in the endoplasmic reticulum. The central, catalytic enzyme of OST is the STT3 subunit, which has homologues in bacteria and archaea. Here we report the X-ray structure of a bacterial OST, the PglB protein of Campylobacter lari, in complex with an acceptor peptide. The structure defines the fold of STT3 proteins and provides insight into glycosylation sequon recognition and amide nitrogen activation, both of which are prerequisites for the formation of the N-glycosidic linkage. We also identified and validated catalytically important, acidic amino acid residues. Our results provide the molecular basis for understanding the mechanism of N-linked glycosylation.

PubMed: 21677752
DOI: 10.1038/nature10151

実験手法

X-RAY DIFFRACTION (3.4 Å)