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TitleStructure, sequon recognition and mechanism of tryptophan C-mannosyltransferase.
Journal, issue, pagesNat Chem Biol, Vol. 19, Issue 5, Page 575-584, Year 2023
Publish dateJan 5, 2023
AuthorsJoël S Bloch / Alan John / Runyu Mao / Somnath Mukherjee / Jérémy Boilevin / Rossitza N Irobalieva / Tamis Darbre / Nichollas E Scott / Jean-Louis Reymond / Anthony A Kossiakoff / Ethan D Goddard-Borger / Kaspar P Locher /
PubMed AbstractC-linked glycosylation is essential for the trafficking, folding and function of secretory and transmembrane proteins involved in cellular communication processes. The tryptophan C- ...C-linked glycosylation is essential for the trafficking, folding and function of secretory and transmembrane proteins involved in cellular communication processes. The tryptophan C-mannosyltransferase (CMT) enzymes that install the modification attach a mannose to the first tryptophan of WxxW/C sequons in nascent polypeptide chains by an unknown mechanism. Here, we report cryogenic-electron microscopy structures of Caenorhabditis elegans CMT in four key states: apo, acceptor peptide-bound, donor-substrate analog-bound and as a trapped ternary complex with both peptide and a donor-substrate mimic bound. The structures indicate how the C-mannosylation sequon is recognized by this CMT and its paralogs, and how sequon binding triggers conformational activation of the donor substrate: a process relevant to all glycosyltransferase C superfamily enzymes. Our structural data further indicate that the CMTs adopt an unprecedented electrophilic aromatic substitution mechanism to enable the C-glycosylation of proteins. These results afford opportunities for understanding human disease and therapeutic targeting of specific CMT paralogs.
External linksNat Chem Biol / PubMed:36604564 / PubMed Central
MethodsEM (single particle)
Resolution2.72 - 3.63 Å
Structure data

14779

7zlg

EMDB-14779, PDB-7zlg:
Cryo-EM structure of C-mannosyltransferase CeDPY19, in complex with acceptor peptide and bound to CMT2-Fab and anti-Fab nanobody
Method: EM (single particle) / Resolution: 2.72 Å

14780

7zlh

EMDB-14780, PDB-7zlh:
Cryo-EM structure of C-mannosyltransferase CeDPY19, in apo state, bound to CMT2-Fab and anti-Fab nanobody
Method: EM (single particle) / Resolution: 2.75 Å

14781

7zli

EMDB-14781, PDB-7zli:
Cryo-EM structure of C-mannosyltransferase CeDPY19, in complex with Dol25-P-Man and bound to CMT2-Fab and anti-Fab nanobody
Method: EM (single particle) / Resolution: 2.99 Å

14782

7zlj

EMDB-14782, PDB-7zlj:
Cryo-EM structure of C-mannosyltransferase CeDPY19, in ternary complex with Dol25-P-C-Man and acceptor peptide, bound to CMT2-Fab and anti-Fab nanobody
Method: EM (single particle) / Resolution: 3.63 Å

Chemicals

ChemComp-HOH:
WATER

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-IZU:
[(2~{R},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]methyl-[(3~{S},6~{E},10~{Z},14~{E})-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraenoxy]phosphinic acid

Source
  • caenorhabditis elegans (invertebrata)
  • synthetic construct (others)
KeywordsMEMBRANE PROTEIN / C-mannosyltransferase

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