6U4B
WbbM bifunctional glycosytransferase apo structure
Summary for 6U4B
| Entry DOI | 10.2210/pdb6u4b/pdb |
| Descriptor | WbbM protein, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | glycsoyltransferase, bifunctional, trimeric, wbbm, duf4422, transferase |
| Biological source | Klebsiella pneumoniae |
| Total number of polymer chains | 1 |
| Total formula weight | 69746.27 |
| Authors | Kimber, M.S.,Mallette, E.,Kamski-Hennekam, E.R.,Gitalis, R. (deposition date: 2019-08-25, release date: 2020-01-22, Last modification date: 2024-03-13) |
| Primary citation | Clarke, B.R.,Ovchinnikova, O.G.,Sweeney, R.P.,Kamski-Hennekam, E.R.,Gitalis, R.,Mallette, E.,Kelly, S.D.,Lowary, T.L.,Kimber, M.S.,Whitfield, C. A bifunctional O-antigen polymerase structure reveals a new glycosyltransferase family. Nat.Chem.Biol., 16:450-457, 2020 Cited by PubMed Abstract: Lipopolysaccharide O-antigen is an attractive candidate for immunotherapeutic strategies targeting antibiotic-resistant Klebsiella pneumoniae. Several K. pneumoniae O-serotypes are based on a shared O2a-antigen backbone repeating unit: (→ 3)-α-Galp-(1 → 3)-β-Galf-(1 →). O2a antigen is synthesized on undecaprenol diphosphate in a pathway involving the O2a polymerase, WbbM, before its export by an ATP-binding cassette transporter. This dual domain polymerase possesses a C-terminal galactopyranosyltransferase resembling known GT8 family enzymes, and an N-terminal DUF4422 domain identified here as a galactofuranosyltransferase defining a previously unrecognized family (GT111). Functional assignment of DUF4422 explains how galactofuranose is incorporated into various polysaccharides of importance in vaccine production and the food industry. In the 2.1-Å resolution structure, three WbbM protomers associate to form a flattened triangular prism connected to a central stalk that orients the active sites toward the membrane. The biochemical, structural and topological properties of WbbM offer broader insight into the mechanisms of assembly of bacterial cell-surface glycans. PubMed: 32152541DOI: 10.1038/s41589-020-0494-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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