Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structures of ALG3/9/12 reveal the assembly logic of the N-glycan oligomannose core.
Journal, issue, pages	Nat Chem Biol, Year 2026
Publish date	Mar 10, 2026
Authors	J Andrew N Alexander / Shu-Yu Chen / Somnath Mukherjee / Mario de Capitani / Rossitza N Irobalieva / Lorenzo Rossi / Parth Agrawal / Julia Kowal / Matheus A Meirelles / Markus Aebi / Jean-Louis Reymond / Anthony A Kossiakoff / Sereina Riniker / Kaspar P Locher /
PubMed Abstract	Asparagine-linked glycans are essential for the maturation and function of most eukaryotic secretory proteins. The biosynthesis and transfer of dolichylpyrophosphate-anchored GlcNAcManGlc glycan is a ...Asparagine-linked glycans are essential for the maturation and function of most eukaryotic secretory proteins. The biosynthesis and transfer of dolichylpyrophosphate-anchored GlcNAcManGlc glycan is a highly conserved process occurring in the endoplasmic reticulum (ER) membrane and involving over a dozen membrane proteins whose dysfunction is linked to congenital disorders of glycosylation (CDGs). Three membrane-integral mannosyltransferases, ALG3, ALG9 and ALG12, mediate four consecutive mannosylation reactions that convert GlcNAcMan to GlcNAcMan. Here, using chemoenzymatically synthesized lipid-linked glycan donor and acceptor analogs, we recapitulated this biosynthetic pathway in vitro. High-resolution cryo-electron microscopy structures of pseudo-Michaelis complexes of each step revealed how the branched glycan is accurately synthesized and unwanted side products are averted. Molecular dynamics simulations and mutagenesis studies uncovered a subtle but precise mechanism selecting the dolichylphosphomannose donor substrate over dolichylphosphoglucose, which is also present in the ER membrane. Our results also provide mechanistic explanations for enzyme dysfunction in CDGs and offer opportunities for N-glycan engineering.
External links	Nat Chem Biol / PubMed:41807832
Methods	EM (single particle)
Resolution	2.42 - 3.08 Å
Structure data	54629 9s6r EMDB-54629, PDB-9s6r: Ternary cryo-EM structure of yeast ALG3 with Dol25-PP-GlcNAc2Man5, Dol25-P-Man, and Fab Method: EM (single particle) / Resolution: 3.08 Å 54630 9s6s EMDB-54630, PDB-9s6s: Ternary cryo-EM structure of human ALG9 with Dol25-PP-GlcNAc2Man6, Dol25-P-Man and Fab Method: EM (single particle) / Resolution: 2.89 Å 54631 9s6t EMDB-54631, PDB-9s6t: Ternary cryo-EM structure of chicken ALG12 with Dol25-PP-GlcNAc2Man7, Dol25-P-Man, and Fab Method: EM (single particle) / Resolution: 2.42 Å 54632 9s6u EMDB-54632, PDB-9s6u: Ternary cryo-EM structure of human ALG9 with Dol25-PP-GlcNAc2Man8, Dol25-P-Man and Fab Method: EM (single particle) / Resolution: 2.95 Å
Chemicals	PDB-1jma: CRYSTAL STRUCTURE OF THE HERPES SIMPLEX VIRUS GLYCOPROTEIN D BOUND TO THE CELLULAR RECEPTOR HVEA/HVEM ChemComp-Y01: CHOLESTEROL HEMISUCCINATE ChemComp-IZY: [(2~{S},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl] [(3~{S},6~{Z},10~{E},14~{E})-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraenyl] hydrogen phosphate ChemComp-HOH: WATER PDB-1jmt: X-ray Structure of a Core U2AF65/U2AF35 Heterodimer ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose PDB-1jmc: SINGLE STRANDED DNA-BINDING DOMAIN OF HUMAN REPLICATION PROTEIN A BOUND TO SINGLE STRANDED DNA, RPA70 SUBUNIT, RESIDUES 183-420 ChemComp-AV0: Lauryl Maltose Neopentyl Glycol PDB-1jmb: CRYSTAL STRUCTURE OF FOUR-HELIX BUNDLE MODEL
Source	Lama glama (llama) synthetic construct (others) saccharomyces cerevisiae (brewer's yeast) homo sapiens (human) gallus gallus (chicken)
Keywords	TRANSFERASE / Mannosyltransferase / ternary complex / N-linked glycosylation