9B77
Cryo-EM Structure of the Glycosyltransferase ArnC from Salmonella enterica in the Apo State Determined on Krios microscope
Summary for 9B77
| Entry DOI | 10.2210/pdb9b77/pdb |
| Related | 8VXH |
| EMDB information | 44302 |
| Descriptor | Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase (2 entities in total) |
| Functional Keywords | glycosyltransferase, undecaprenyl phosphate, aminoarabinose, polymyxin resistance, gt-a, transferase |
| Biological source | Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 |
| Total number of polymer chains | 4 |
| Total formula weight | 162902.16 |
| Authors | Ashraf, K.U.,Punetha, A.,Petrou, V.I. (deposition date: 2024-03-27, release date: 2025-02-05, Last modification date: 2025-03-05) |
| Primary citation | Ashraf, K.U.,Bunoro-Batista, M.,Ansell, T.B.,Punetha, A.,Rosario-Garrido, S.,Firlar, E.,Kaelber, J.T.,Stansfeld, P.J.,Petrou, V.I. Structural basis of undecaprenyl phosphate glycosylation leading to polymyxin resistance in Gram-negative bacteria. Biorxiv, 2025 Cited by PubMed Abstract: In Gram-negative bacteria, the enzymatic modification of Lipid A with aminoarabinose (L-Ara4N) leads to resistance against polymyxin antibiotics and cationic antimicrobial peptides. ArnC, an integral membrane glycosyltransferase, attaches a formylated form of aminoarabinose to the lipid undecaprenyl phosphate, enabling its association with the bacterial inner membrane. Here, we present cryo-electron microscopy structures of ArnC from in and nucleotide-bound conformations. These structures reveal a conformational transition that takes place upon binding of the partial donor substrate. Using coarse-grained and atomistic simulations, we provide insights into substrate coordination before and during catalysis, and we propose a catalytic mechanism that may operate on all similar metal-dependent polyprenyl phosphate glycosyltransferases. The reported structures provide a new target for drug design aiming to combat polymyxin resistance. PubMed: 39974898DOI: 10.1101/2025.01.29.634835 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.74 Å) |
Structure validation
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