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TitleMembrane domain structures of three classes of histidine kinase receptors by cell-free expression and rapid NMR analysis.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 107, Page 10902-10907, Year 2010
Publish dateJan 2, 2010 (structure data deposition date)
AuthorsMaslennikov, I. / Klammt, C. / Hwang, E. / Kefala, G. / Okamura, M. / Esquivies, L. / Mors, K. / Glaubitz, C. / Kwiatkowski, W. / Jeon, Y.H. / Choe, S.
External linksProc. Natl. Acad. Sci. USA / PubMed:20498088
MethodsNMR (solution)
Structure data

PDB-2ksd:
Backbone structure of the membrane domain of E. coli histidine kinase receptor ArcB, Center for Structures of Membrane Proteins (CSMP) target 4310C
Method: SOLUTION NMR

PDB-2kse:
Backbone structure of the membrane domain of E. coli histidine kinase receptor QseC, Center for Structures of Membrane Proteins (CSMP) target 4311C
Method: SOLUTION NMR

PDB-2ksf:
Backbone structure of the membrane domain of E. coli histidine kinase receptor KdpD, Center for Structures of Membrane Proteins (CSMP) target 4312C
Method: SOLUTION NMR

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / methods development / Histidine kinase receptor / membrane domain / two-helical hairpin / cell-free synthesis / Cell inner membrane / Cell membrane / Kinase / Transcription / Transcription regulation / Transmembrane / Two-component regulatory system / Structural Genomics / PSI-2 / Protein Structure Initiative / Center for Structures of Membrane Proteins / CSMP / ATP-binding / Membrane / Nucleotide-binding / Phosphoprotein / four-helical bundle

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