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6EJK

Structure of a glycosyltransferase

Summary for 6EJK
Entry DOI10.2210/pdb6ejk/pdb
Related6EJJ
DescriptorWlaC protein, 2-acetamido-2-deoxy-alpha-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-alpha-D-glucopyranose, Uridine-Diphosphate-Methylene-N-acetyl-galactosamine, ... (4 entities in total)
Functional Keywordsglycosyltransferase, transferase
Biological sourceCampylobacter jejuni
Total number of polymer chains2
Total formula weight89877.78
Authors
Ramirez, A.S.,Boilevin, J.,Mehdipour, A.R.,Hummer, G.,Darbre, T.,Reymond, J.L.,Locher, K.P. (deposition date: 2017-09-21, release date: 2018-02-07, Last modification date: 2024-01-17)
Primary citationRamirez, A.S.,Boilevin, J.,Mehdipour, A.R.,Hummer, G.,Darbre, T.,Reymond, J.L.,Locher, K.P.
Structural basis of the molecular ruler mechanism of a bacterial glycosyltransferase.
Nat Commun, 9:445-445, 2018
Cited by
PubMed Abstract: The membrane-associated, processive and retaining glycosyltransferase PglH from Campylobacter jejuni is part of the biosynthetic pathway of the lipid-linked oligosaccharide (LLO) that serves as the glycan donor in bacterial protein N-glycosylation. Using an unknown counting mechanism, PglH catalyzes the transfer of exactly three α1,4 N-acetylgalactosamine (GalNAc) units to the growing LLO precursor, GalNAc-α1,4-GalNAc-α1,3-Bac-α1-PP-undecaprenyl. Here, we present crystal structures of PglH in three distinct states, including a binary complex with UDP-GalNAc and two ternary complexes containing a chemo-enzymatically generated LLO analog and either UDP or synthetic, nonhydrolyzable UDP-CH-GalNAc. PglH contains an amphipathic helix ("ruler helix") that has a dual role of facilitating membrane attachment and glycan counting. The ruler helix contains three positively charged side chains that can bind the pyrophosphate group of the LLO substrate and thus limit the addition of GalNAc units to three. These results, combined with molecular dynamics simulations, provide the mechanism of glycan counting by PglH.
PubMed: 29386647
DOI: 10.1038/s41467-018-02880-2
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.3 Å)
Structure validation

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