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5aex

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Crystal structure of Saccharomyces cerevisiae Mep2Crystal structure of Saccharomyces cerevisiae Mep2

Structural highlights

5aex is a 9 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[MEP2_YEAST] Transporter for ammonium (both charged and uncharged NH3 and NH4) to use as a nitrogen source. The affinity of MEP2 is about twenty times higher than that of MEP1. MEP3 has the lowest affinity. Under ammonium limitation acts as an ammonium sensor, generating a signal that leads to pseudohyphal growth.[1] [2] [3] [4]

References

  1. ↑ Marini AM, Andre B. In vivo N-glycosylation of the mep2 high-affinity ammonium transporter of Saccharomyces cerevisiae reveals an extracytosolic N-terminus. Mol Microbiol. 2000 Nov;38(3):552-64. PMID:11069679
  2. ↑ Soupene E, Ramirez RM, Kustu S. Evidence that fungal MEP proteins mediate diffusion of the uncharged species NH(3) across the cytoplasmic membrane. Mol Cell Biol. 2001 Sep;21(17):5733-41. PMID:11486013
  3. ↑ Marini AM, Soussi-Boudekou S, Vissers S, Andre B. A family of ammonium transporters in Saccharomyces cerevisiae. Mol Cell Biol. 1997 Aug;17(8):4282-93. PMID:9234685
  4. ↑ Lorenz MC, Heitman J. The MEP2 ammonium permease regulates pseudohyphal differentiation in Saccharomyces cerevisiae. EMBO J. 1998 Aug 10;17(5):1236-47. PMID:9482721 doi:http://dx.doi.org/10.1093/emboj/17.5.1236

5aex, resolution 3.20Å

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