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TitleATPase Active-Site Electrostatic Interactions Control the Global Conformation of the 100 kDa SecA Translocase.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 135, Page 2999-3010, Year 2013
Publish dateAug 20, 2009 (structure data deposition date)
AuthorsKim, D.M. / Zheng, H. / Huang, Y.J. / Montelione, G.T. / Hunt, J.F.
External linksJ. Am. Chem. Soc. / PubMed:23167435
MethodsX-ray diffraction
Resolution3.3 - 3.4 Å
Structure data

PDB-3iqm:
Active site mutants of B. subtilis SecA
Method: X-RAY DIFFRACTION / Resolution: 3.4 Å

PDB-3iqy:
Active site mutants of B. subtilis SecA
Method: X-RAY DIFFRACTION / Resolution: 3.3 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • bacillus subtilis subsp. subtilis (bacteria)
  • bacillus subtilis (bacteria)
KeywordsPROTEIN TRANSPORT / alpha-beta protein / ATP-binding / Cell membrane / Membrane / Metal-binding / Nucleotide-binding / Translocation / Transport / alpha beta

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