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Structure paper

TitleStructural Basis for Mep2 Ammonium Transceptor Activation by Phosphorylation.
Journal, issue, pagesNat. Commun., Vol. 7, Page 11337-, Year 2016
Publish dateJan 12, 2015 (structure data deposition date)
AuthorsVan Den Berg, B. / Chembath, A. / Jefferies, D. / Basle, A. / Khalid, S. / Rutherford, J.
External linksNat. Commun. / PubMed:27088325
MethodsX-ray diffraction
Resolution1.47 - 3.4 Å
Structure data

PDB-5aex:
Crystal structure of Saccharomyces cerevisiae Mep2
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

PDB-5aez:
Crystal structure of Candida albicans Mep2
Method: X-RAY DIFFRACTION / Resolution: 1.47 Å

PDB-5af1:
Crystal structure of Candida albicans Mep2
Method: X-RAY DIFFRACTION / Resolution: 1.639 Å

PDB-5ah3:
Crystal structure of the Mep2 mutant R452D,S453D from Candida albicans
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-5aid:
Crystal structure of the Mep2 mutant delta442 from Candida albicans
Method: X-RAY DIFFRACTION / Resolution: 3.4 Å

PDB-5fuf:
Crystal structure of the Mep2 mutant S453D from Candida albicans
Method: X-RAY DIFFRACTION / Resolution: 2.066 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-BNG:
nonyl beta-D-glucopyranoside / detergent*YM

ChemComp-HOH:
WATER

ChemComp-DMU:
DECYL-BETA-D-MALTOPYRANOSIDE / detergent*YM

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • candida albicans (yeast)
KeywordsMEMBRANE PROTEIN / AMMONIUM TRANSPORTER / TRANSPORT PROTEIN / MEMBRANE / MEMBRANE PROTEIN AMMONIUM TRANSPORTER MEP2 CANDIDA ALBICANS / MEP2 / TRANSPORT

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