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Structure paper

TitleSubstrate binding, deprotonation, and selectivity at the periplasmic entrance of the Escherichia coli ammonia channel AmtB.
Journal, issue, pagesProc. Natl. Acad. Sci. Usa, Vol. 105, Page 5040-5045, Year 2008
Publish dateJan 23, 2008 (structure data deposition date)
AuthorsJavelle, A. / Lupo, D. / Ripoche, P. / Fulford, T. / Merrick, M. / Winkler, F.K.
External linksProc. Natl. Acad. Sci. Usa / PubMed:18362341
MethodsX-ray diffraction
Resolution2 - 2.3 Å
Structure data

PDB-3c1g:
Substrate binding, deprotonation and selectivity at the periplasmic entrance of the E. coli ammonia channel AmtB
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-3c1h:
Substrate binding, deprotonation and selectivity at the periplasmic entrance of the E. coli ammonia channel AmtB
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-3c1i:
Substrate binding, deprotonation and selectivity at the periplasmic entrance of the E. coli ammonia channel AmtB
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-3c1j:
Substrate binding, deprotonation and selectivity at the periplasmic entrance of the E. coli ammonia channel AmtB
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-LDA:
LAURYL DIMETHYLAMINE-N-OXIDE / LDAO, detergent*YM

ChemComp-IMD:
IMIDAZOLE

ChemComp-GOL:
GLYCEROL

Source
  • escherichia coli (E. coli)
KeywordsTRANSPORT PROTEIN / Membrane Protein / Ammonia Transport / wild-type AmtB / Inner membrane / Transmembrane / Phe-Gate Mutant / AmtB / Phe-gate Double Mutant / Transmembrane'

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