3VU0

Crystal structure of the C-terminal globular domain of oligosaccharyltransferase (AfAglB-S2, AF_0040, O30195_ARCFU) from Archaeoglobus fulgidus

Summary for 3VU0

• Entry DOI: 10.2210/pdb3vu0/pdb
• Related: 3VU1
• Descriptor: Putative uncharacterized protein, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID (3 entities in total)
• Functional Keywords: glycotransferase, asn-glycosylation, membrane, transferase
• Biological source: Archaeoglobus fulgidus
• Total number of polymer chains: 3
• Total formula weight: 59275.77

Authors

Nyirenda, J.,Matsumoto, S.,Saitoh, T.,Maita, N.,Noda, N.N.,Inagaki, F.,Kohda, D. (deposition date: 2012-06-13, release date: 2013-01-23, Last modification date: 2024-10-16)

Primary citation

Nyirenda, J.,Matsumoto, S.,Saitoh, T.,Maita, N.,Noda, N.N.,Inagaki, F.,Kohda, D.
Crystallographic and NMR Evidence for Flexibility in Oligosaccharyltransferases and Its Catalytic Significance
Structure, 21:32-41, 2013

PubMed Abstract: Oligosaccharyltransferase (OST) is a membrane-bound enzyme that catalyzes the transfer of an oligosaccharide to an asparagine residue in glycoproteins. It possesses a binding pocket that recognizes Ser and Thr residues at the +2 position in the N-glycosylation consensus, Asn-X-Ser/Thr. We determined the crystal structures of the C-terminal globular domains of the catalytic subunits of two archaeal OSTs. A comparison with previously determined structures identified a segment with remarkable conformational plasticity, induced by crystal contact effects. We characterized its dynamic properties in solution by (15)N NMR relaxation analyses. Intriguingly, the mobile region contains the +2 Ser/Thr-binding pocket. In agreement, the flexibility restriction forced by an engineered disulfide crosslink abolished the enzymatic activity, and its cleavage fully restored activity. These results suggest the necessity of multiple conformational states in the reaction. The dynamic nature of the Ser/Thr pocket could facilitate the efficient scanning of N-glycosylation sequons along nascent polypeptide chains.

PubMed: 23177926
DOI: 10.1016/j.str.2012.10.011

Experimental method

X-RAY DIFFRACTION (1.94 Å)