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TitleStructural elucidation of the Cys-His-Glu-Asn proteolytic relay in the secreted CHAP domain enzyme from the human pathogen Staphylococcus saprophyticus.
Journal, issue, pagesProteins, Vol. 74, Page 515-519, Year 2008
Publish dateApr 29, 2008 (structure data deposition date)
AuthorsRossi, P. / Aramini, J.M. / Xiao, R. / Chen, C.X. / Nwosu, C. / Owens, L.A. / Maglaqui, M. / Nair, R. / Fischer, M. / Acton, T.B. ...Rossi, P. / Aramini, J.M. / Xiao, R. / Chen, C.X. / Nwosu, C. / Owens, L.A. / Maglaqui, M. / Nair, R. / Fischer, M. / Acton, T.B. / Honig, B. / Rost, B. / Montelione, G.T.
External linksProteins / PubMed:18951393
MethodsNMR (solution)
Structure data

PDB-2k3a:
NMR solution structure of Staphylococcus saprophyticus CHAP (cysteine, histidine-dependent amidohydrolases/peptidases) domain protein. Northeast Structural Genomics Consortium target SyR11
Method: SOLUTION NMR

Source
  • staphylococcus saprophyticus subsp. saprophyticus atcc 15305 (bacteria)
KeywordsHYDROLASE / Protein / monomer / CHAP domain / putative amidase / Structural Genomics / PSI-2 / Protein Structure Initiative / Northeast Structural Genomics Consortium / NESG / HYDROLASE ANTIGEN

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