5ah3

Crystal structure of the Mep2 mutant R452D,S453D from Candida albicans

spinqualitylabelsall models 5ah3, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ah3 is a 1 chain structure with sequence from Candida albicans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: DMU Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q59UP8_CANAL Publication Abstract from PubMed 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 approximately 30 A 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. Structural basis for Mep2 ammonium transceptor activation by phosphorylation.,van den Berg B, Chembath A, Jefferies D, Basle A, Khalid S, Rutherford JC Nat Commun. 2016 Apr 18;7:11337. doi: 10.1038/ncomms11337. PMID:27088325 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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