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TitleStructural characterization of Spo0E-like protein-aspartic acid phosphatases that regulate sporulation in bacilli.
Journal, issue, pagesJ. Biol. Chem., Vol. 281, Page 37993-38003, Year 2006
Publish dateAug 14, 2005 (structure data deposition date)
AuthorsGrenha, R. / Rzechorzek, N.J. / Brannigan, J.A. / de Jong, R.N. / Ab, E. / Diercks, T. / Truffault, V. / Ladds, J.C. / Fogg, M.J. / Bongiorni, C. ...Grenha, R. / Rzechorzek, N.J. / Brannigan, J.A. / de Jong, R.N. / Ab, E. / Diercks, T. / Truffault, V. / Ladds, J.C. / Fogg, M.J. / Bongiorni, C. / Perego, M. / Kaptein, R. / Wilson, K.S. / Folkers, G.E. / Wilkinson, A.J.
External linksJ. Biol. Chem. / PubMed:17001075
MethodsNMR (solution)
Structure data

PDB-2bzb:
NMR Solution Structure of a protein aspartic acid phosphate phosphatase from Bacillus Anthracis
Method: SOLUTION NMR

PDB-2c0s:
NMR Solution Structure of a protein aspartic acid phosphate phosphatase from Bacillus Anthracis
Method: SOLUTION NMR

Source
  • bacillus anthracis (anthrax bacterium)
  • bacillus anthracis str. ames (bacteria)
KeywordsTRANSFERASE / PHOSPHATASE / PHOSPHORYLATION / SPORULATION / BACILLUS / ANTHRACIS / ANTITHETICAL / NEGATIVE / REGULATOR / SPINE / BACILLUS ANTHRACIS / NEGATIVE REGULATOR

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