3AAG

Crystal structure of C. jejuni pglb C-terminal domain

3AAG の概要

• エントリーDOI: 10.2210/pdb3aag/pdb
• 分子名称: General glycosylation pathway protein, CALCIUM ION (2 entities in total)
• 機能のキーワード: multidomain, transferase
• 由来する生物種: Campylobacter jejuni
• 細胞内の位置: Cell inner membrane ; Multi- pass membrane protein : Q5HTX9
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68449.97

構造登録者

Maita, N.,Kohda, D. (登録日: 2009-11-16, 公開日: 2009-12-08, 最終更新日: 2025-03-26)

主引用文献

Maita, N.,Nyirenda, J.,Igura, M.,Kamishikiryo, J.,Kohda, D.
Comparative structural biology of Eubacterial and Archaeal oligosaccharyltransferases.
J.Biol.Chem., 285:4941-4950, 2010

PubMed Abstract: Oligosaccharyltransferase (OST) catalyzes the transfer of an oligosaccharide from a lipid donor to an asparagine residue in nascent polypeptide chains. In the bacterium Campylobacter jejuni, a single-subunit membrane protein, PglB, catalyzes N-glycosylation. We report the 2.8 A resolution crystal structure of the C-terminal globular domain of PglB and its comparison with the previously determined structure from the archaeon Pyrococcus AglB. The two distantly related oligosaccharyltransferases share unexpected structural similarity beyond that expected from the sequence comparison. The common architecture of the putative catalytic sites revealed a new catalytic motif in PglB. Site-directed mutagenesis analyses confirmed the contribution of this motif to the catalytic function. Bacterial PglB and archaeal AglB constitute a protein family of the catalytic subunit of OST along with STT3 from eukaryotes. A structure-aided multiple sequence alignment of the STT3/PglB/AglB protein family revealed three types of OST catalytic centers. This novel classification will provide a useful framework for understanding the enzymatic properties of the OST enzymes from Eukarya, Archaea, and Bacteria.

PubMed: 20007322
DOI: 10.1074/jbc.M109.081752

実験手法

X-RAY DIFFRACTION (2.8 Å)