7E9S

Archaeal oligosaccharyltransferase AglB from Archaeoglobus fulgidus in complex with an inhibitory peptide and a dolichol-phosphate

Summary for 7E9S

• Entry DOI: 10.2210/pdb7e9s/pdb
• Descriptor: Dolichyl-phosphooligosaccharide-protein glycotransferase 3, a polypeptide linked to an inhibitory N-glycosylation sequon-containing peptide, MANGANESE (II) ION, ... (7 entities in total)
• Functional Keywords: protein n-glycosylation, ternary complex, sequon-containing peptide, dolichol-phosphate, transferase
• Biological source: Archaeoglobus fulgidus DSM 4304; More
• Total number of polymer chains: 2
• Total formula weight: 102938.84

Authors

Taguchi, Y.,Hirata, K.,Kohda, D. (deposition date: 2021-03-05, release date: 2021-09-08, Last modification date: 2024-10-23)

Primary citation

Taguchi, Y.,Yamasaki, T.,Ishikawa, M.,Kawasaki, Y.,Yukimura, R.,Mitani, M.,Hirata, K.,Kohda, D.
The structure of an archaeal oligosaccharyltransferase provides insight into the strict exclusion of proline from the N-glycosylation sequon.
Commun Biol, 4:941-941, 2021

PubMed Abstract: Oligosaccharyltransferase (OST) catalyzes oligosaccharide transfer to the Asn residue in the N-glycosylation sequon, Asn-X-Ser/Thr, where Pro is strictly excluded at position X. Considering the unique structural properties of proline, this exclusion may not be surprising, but the structural basis for the rejection of Pro residues should be explained explicitly. Here we determined the crystal structure of an archaeal OST in a complex with a sequon-containing peptide and dolichol-phosphate to a 2.7 Å resolution. The sequon part in the peptide forms two inter-chain hydrogen bonds with a conserved amino acid motif, TIXE. We confirmed the essential role of the TIXE motif and the adjacent regions by extensive alanine-scanning of the external loop 5. A Ramachandran plot revealed that the ring structure of the Pro side chain is incompatible with the ϕ backbone dihedral angle around -150° in the rigid sequon-TIXE structure. The present structure clearly provides the structural basis for the exclusion of Pro residues from the N-glycosylation sequon.

PubMed: 34354228
DOI: 10.1038/s42003-021-02473-8

Experimental method

X-RAY DIFFRACTION (2.7 Å)