3WAI

Crystal structure of the C-terminal globular domain of oligosaccharyltransferase (AfAglB-L, O29867_ARCFU) from Archaeoglobus fulgidus as a MBP fusion

Summary for 3WAI

Entry DOI	10.2210/pdb3wai/pdb
Related	3WAJ 3WAK
Descriptor	Maltose-binding periplasmic protein, Transmembrane oligosaccharyl transferase (2 entities in total)
Functional Keywords	oligosaccharyltransferase, n-glycosylation, mbp fusion, gt-c, protein b-oligosaccharyltransferase, transferase, transport protein
Biological source	Escherichia coli More
Total number of polymer chains	1
Total formula weight	82973.31
Authors	Matsumoto, S.,Shimada, A.,Kohda, D. (deposition date: 2013-05-03, release date: 2013-07-17, Last modification date: 2023-11-08)
Primary citation	Matsumoto, S.,Shimada, A.,Kohda, D. Crystal structure of the C-terminal globular domain of the third paralog of the Archaeoglobus fulgidus oligosaccharyltransferases Bmc Struct.Biol., 13:11-11, 2013 Cited by PubMed Abstract: Protein N-glycosylation occurs in the three domains of life. Oligosaccharyltransferase (OST) transfers an oligosaccharide chain to the asparagine residue in the N-glycosylation sequons. The catalytic subunits of the OST enzyme are STT3 in eukaryotes, AglB in archaea and PglB in eubacteria. The genome of a hyperthermophilic archaeon, Archaeoglobus fulgidus, encodes three paralogous AglB proteins. We previously solved the crystal structures of the C-terminal globular domains of two paralogs, AglB-Short 1 and AglB-Short 2. PubMed: 23815857 DOI: 10.1186/1472-6807-13-11 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.897 Å)

Structure validation