5AH3
Crystal structure of the Mep2 mutant R452D,S453D from Candida albicans
Summary for 5AH3
| Entry DOI | 10.2210/pdb5ah3/pdb |
| Descriptor | MEP2, DECYL-BETA-D-MALTOPYRANOSIDE (3 entities in total) |
| Functional Keywords | transport protein, membrane, membrane protein ammonium transporter mep2 candida albicans |
| Biological source | CANDIDA ALBICANS |
| Cellular location | Membrane ; Multi-pass membrane protein : Q59UP8 |
| Total number of polymer chains | 1 |
| Total formula weight | 55188.14 |
| Authors | van den Berg, B.,Chembath, A.,Rutherford, J. (deposition date: 2015-02-04, release date: 2016-03-02, Last modification date: 2024-01-10) |
| Primary citation | Van Den Berg, B.,Chembath, A.,Jefferies, D.,Basle, A.,Khalid, S.,Rutherford, J. Structural Basis for Mep2 Ammonium Transceptor Activation by Phosphorylation. Nat.Commun., 7:11337-, 2016 Cited by PubMed Abstract: Mep2 proteins are fungal transceptors that play an important role as ammonium sensors in fungal development. Mep2 activity is tightly regulated by phosphorylation, but how this is achieved at the molecular level is not clear. Here we report X-ray crystal structures of the Mep2 orthologues from Saccharomyces cerevisiae and Candida albicans and show that under nitrogen-sufficient conditions the transporters are not phosphorylated and present in closed, inactive conformations. Relative to the open bacterial ammonium transporters, non-phosphorylated Mep2 exhibits shifts in cytoplasmic loops and the C-terminal region (CTR) to occlude the cytoplasmic exit of the channel and to interact with His2 of the twin-His motif. The phosphorylation site in the CTR is solvent accessible and located in a negatively charged pocket ∼30 Å away from the channel exit. The crystal structure of phosphorylation-mimicking Mep2 variants from C. albicans show large conformational changes in a conserved and functionally important region of the CTR. The results allow us to propose a model for regulation of eukaryotic ammonium transport by phosphorylation. PubMed: 27088325DOI: 10.1038/NCOMMS11337 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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