2pii
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PII, GLNB PRODUCT
OverviewOverview
The structure of the bacterial signal transduction protein P(II) has been, refined to an R factor of 13.2% using 3sigma data between 10 and 1.9 A., 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 A structure, [Cheah, Carr, Suffolk, Vasudevan, Dixon & Ollis (1994). Structure, 2, 981-990] served as a starting model. P(II) 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 A model, although it leads to a redefinition of the extent of various, secondary-structural elements. The monomeric structure of P(II) exhibits, an interlocking double betaalphabeta 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.
About this StructureAbout this Structure
2PII is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
X-ray structure of the signal transduction protein from Escherichia coli at 1.9 A., Carr PD, Cheah E, Suffolk PM, Vasudevan SG, Dixon NE, Ollis DL, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):93-104. PMID:15299730
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