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| | <StructureSection load='5aid' size='340' side='right'caption='[[5aid]], [[Resolution|resolution]] 3.40Å' scene=''> | | <StructureSection load='5aid' size='340' side='right'caption='[[5aid]], [[Resolution|resolution]] 3.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5aid]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11006_[[monilia_stellatoidea]] Atcc 11006 [[monilia stellatoidea]]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AID OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AID FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5aid]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AID FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5aid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aid OCA], [http://pdbe.org/5aid PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aid RCSB], [http://www.ebi.ac.uk/pdbsum/5aid PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5aid ProSAT]</span></td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5aid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aid OCA], [https://pdbe.org/5aid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aid RCSB], [https://www.ebi.ac.uk/pdbsum/5aid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aid ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q59UP8_CANAL Q59UP8_CANAL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Candida albicans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Berg, B van den]]
| + | [[Category: Chembath A]] |
| - | [[Category: Chembath, A]] | + | [[Category: Rutherford J]] |
| - | [[Category: Rutherford, J]] | + | [[Category: Van den Berg B]] |
| - | [[Category: Ammonium transporter]] | + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Mep2]]
| + | |
| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ van den Berg B, Chembath A, Jefferies D, Basle A, Khalid S, Rutherford JC. Structural basis for Mep2 ammonium transceptor activation by phosphorylation. Nat Commun. 2016 Apr 18;7:11337. doi: 10.1038/ncomms11337. PMID:27088325 doi:http://dx.doi.org/10.1038/ncomms11337
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