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X-ray structure of the signal transduction protein PII from Escherichia coli at 1.9 Å

Journal Article


Abstract


  • The structure of the bacterial signal transduction protein PII has been refined to an R factor of 13.2% using 3σ data between 10 and 1.9 Å. The crystals exhibited twinning by merohedry and X-ray intensities were corrected using the method of Fisher & Sweet [Fisher & Sweet (1980). Acta Cryst. A36, 755-760] prior to refinement. Our earlier 2.7 Å structure [Cheah, Carr, Suffolk, Vasudevan, Dixon & Ollis (1994). Structure, 2, 981-990] served as a starting model. PII is a trimeric molecule, each subunit has a mass of 12.4 kDa and contains 112 amino-acid residues. The refined model includes all 1065 protein atoms per subunit plus 312 water molecules. The high-resolution refinement confirms the correctness of our 2.7 Å model, although it leads to a redefinition of the extent of various secondary-structural elements. The monomeric structure of PII exhibits an interlocking dou-ble βαβ fold. This is a stable fold found in a number of proteins with diverse functions. The association of the protein into a trimer leads to a new structure which we describe in detail. The effects of crystal packing forces are discussed and potential interaction sites with other proteins and effector molecules are identified.

Publication Date


  • 1996

Citation


  • Carr, P. D., Cheah, E., Suffolk, P. M., Vasudevan, S. G., Dixon, N. E., & Ollis, D. L. (1996). X-ray structure of the signal transduction protein PII from Escherichia coli at 1.9 Å. Acta Crystallographica Section D: Biological Crystallography, 52(1), 93-104. doi:10.1107/S0907444995007293

Scopus Eid


  • 2-s2.0-0030040863

Start Page


  • 93

End Page


  • 104

Volume


  • 52

Issue


  • 1

Abstract


  • The structure of the bacterial signal transduction protein PII has been refined to an R factor of 13.2% using 3σ data between 10 and 1.9 Å. The crystals exhibited twinning by merohedry and X-ray intensities were corrected using the method of Fisher & Sweet [Fisher & Sweet (1980). Acta Cryst. A36, 755-760] prior to refinement. Our earlier 2.7 Å structure [Cheah, Carr, Suffolk, Vasudevan, Dixon & Ollis (1994). Structure, 2, 981-990] served as a starting model. PII is a trimeric molecule, each subunit has a mass of 12.4 kDa and contains 112 amino-acid residues. The refined model includes all 1065 protein atoms per subunit plus 312 water molecules. The high-resolution refinement confirms the correctness of our 2.7 Å model, although it leads to a redefinition of the extent of various secondary-structural elements. The monomeric structure of PII exhibits an interlocking dou-ble βαβ fold. This is a stable fold found in a number of proteins with diverse functions. The association of the protein into a trimer leads to a new structure which we describe in detail. The effects of crystal packing forces are discussed and potential interaction sites with other proteins and effector molecules are identified.

Publication Date


  • 1996

Citation


  • Carr, P. D., Cheah, E., Suffolk, P. M., Vasudevan, S. G., Dixon, N. E., & Ollis, D. L. (1996). X-ray structure of the signal transduction protein PII from Escherichia coli at 1.9 Å. Acta Crystallographica Section D: Biological Crystallography, 52(1), 93-104. doi:10.1107/S0907444995007293

Scopus Eid


  • 2-s2.0-0030040863

Start Page


  • 93

End Page


  • 104

Volume


  • 52

Issue


  • 1