Protein Family Models

Date:

2024-08-14

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. Structural analysis of a bacterial OST, undecaprenyl-diphosphooligosaccharide protein glycotransferase EC:2.4.99.19 (PglB) protein, revealed two domains: a transmembrane domain and a periplasmic domain. This entry represents the C-terminal periplasmic beta-barrel domain [1]. [1]. 21677752. X-ray structure of a bacterial oligosaccharyltransferase.. Lizak C, Gerber S, Numao S, Aebi M, Locher KP;. Nature. 2011;474:350-355. (from Pfam)

Date:

2024-08-14

This entry consists of the oligosaccharyl transferase STT3 subunit and related proteins. The STT3 subunit is part of the oligosaccharyl transferase (OTase) complex of proteins and is required for its activity [2]. In eukaryotes, OTase transfers a lipid-linked core-oligosaccharide to selected asparagine residues in the ER [2]. In the archaea STT3 occurs alone, rather than in an OTase complex, and is required for N-glycosylation of asparagines [3-4]. This entry represents the N-terminal domain, consisting of transmembrane helices. [1]. 8838310. Molecular cloning of a highly conserved mouse and human integral. membrane protein (Itm1) and genetic mapping to mouse chromosome. 9.. Hong G, Deleersnijder W, Kozak CA, Van Marck E, Tylzanowski P,. Merregaert J;. Genomics 1996;31:295-300.. [2]. 7588624. STT3, a highly conserved protein required for yeast. oligosaccharyl transferase activity in vivo.. Zufferey R, Knauer R, Burda P, Stagljar I, te Heesen S, Lehle L,. Aebi M;. EMBO J 1995;14:4949-4960.. [3]. 17996897. Haloferax volcanii AglB and AglD are involved in N-glycosylation. of the S-layer glycoprotein and proper assembly of the surface. layer.. Abu-Qarn M, Yurist-Doutsch S, Giordano A, Trauner A, Morris HR,. Hitchen P, Medalia O, Dell A, Eichler J;. J Mol Biol. 2007;374:1224-1236.. [4]. 18046457. Structure-guided identification of a new catalytic motif of. oligosaccharyltransferase.. Igura M, Maita N, Kamishikiryo J, Yamada M, Obita T, Maenaka K,. Kohda D;. EMBO J. 2008;27:234-243. (from Pfam)

Date:

2024-08-14