5F15
Crystal Structure of ArnT from Cupriavidus metallidurans bound to Undecaprenyl phosphate
Summary for 5F15
| Entry DOI | 10.2210/pdb5f15/pdb |
| Related | 5EZM |
| Descriptor | 4-amino-4-deoxy-L-arabinose (L-Ara4N) transferase, [(Z)-octadec-9-enyl] (2R)-2,3-bis(oxidanyl)propanoate, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (7 entities in total) |
| Functional Keywords | membrane protein, lipid glycosyltransferase, gt-c fold, undecaprenyl phosphate, structural genomics, psi-biology, new york consortium on membrane protein structure, nycomps, transferase |
| Biological source | Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) |
| Total number of polymer chains | 1 |
| Total formula weight | 91560.84 |
| Authors | Petrou, V.I.,Clarke, O.B.,Tomasek, D.,Banerjee, S.,Rajashankar, K.R.,Mancia, F.,New York Consortium on Membrane Protein Structure (NYCOMPS) (deposition date: 2015-11-30, release date: 2016-02-17, Last modification date: 2024-03-06) |
| Primary citation | Petrou, V.I.,Herrera, C.M.,Schultz, K.M.,Clarke, O.B.,Vendome, J.,Tomasek, D.,Banerjee, S.,Rajashankar, K.R.,Belcher Dufrisne, M.,Kloss, B.,Kloppmann, E.,Rost, B.,Klug, C.S.,Trent, M.S.,Shapiro, L.,Mancia, F. Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation. Science, 351:608-612, 2016 Cited by PubMed Abstract: Polymyxins are antibiotics used in the last line of defense to combat multidrug-resistant infections by Gram-negative bacteria. Polymyxin resistance arises through charge modification of the bacterial outer membrane with the attachment of the cationic sugar 4-amino-4-deoxy-l-arabinose to lipid A, a reaction catalyzed by the integral membrane lipid-to-lipid glycosyltransferase 4-amino-4-deoxy-L-arabinose transferase (ArnT). Here, we report crystal structures of ArnT from Cupriavidus metallidurans, alone and in complex with the lipid carrier undecaprenyl phosphate, at 2.8 and 3.2 angstrom resolution, respectively. The structures show cavities for both lipidic substrates, which converge at the active site. A structural rearrangement occurs on undecaprenyl phosphate binding, which stabilizes the active site and likely allows lipid A binding. Functional mutagenesis experiments based on these structures suggest a mechanistic model for ArnT family enzymes. PubMed: 26912703DOI: 10.1126/science.aad1172 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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