5aex: Difference between revisions

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'''Unreleased structure'''
==Crystal structure of Saccharomyces cerevisiae Mep2==
 
<StructureSection load='5aex' size='340' side='right' caption='[[5aex]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
The entry 5aex is ON HOLD  until Paper Publication
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5aex]] is a 9 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AEX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AEX FirstGlance]. <br>
Authors: Rutherford, J.C., Chembath, A., van den Berg, B.
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
 
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5aez|5aez]], [[5af1|5af1]]</td></tr>
Description: Crystal structure of Saccharomyces cerevisiae Mep2
<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=5aex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aex OCA], [http://pdbe.org/5aex PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aex RCSB], [http://www.ebi.ac.uk/pdbsum/5aex PDBsum]</span></td></tr>
[[Category: Unreleased Structures]]
</table>
[[Category: Van Den Berg, B]]
== Function ==
[[http://www.uniprot.org/uniprot/MEP2_YEAST 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.<ref>PMID:11069679</ref> <ref>PMID:11486013</ref> <ref>PMID:9234685</ref> <ref>PMID:9482721</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Berg, B van den]]
[[Category: Chembath, A]]
[[Category: Chembath, A]]
[[Category: Rutherford, J.C]]
[[Category: Rutherford, J C]]
[[Category: Membrane protein]]

Revision as of 20:16, 20 January 2016

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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