2PII

PII, GLNB PRODUCT

Summary for 2PII

• Entry DOI: 10.2210/pdb2pii/pdb
• Descriptor: PII (2 entities in total)
• Functional Keywords: signal transduction protein
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 12443.44

Authors

Carr, P.D.,Cheah, E.,Suffolk, P.M.,Ollis, D.L. (deposition date: 1995-05-02, release date: 1996-06-20, Last modification date: 2024-02-21)

Primary citation

Carr, P.D.,Cheah, E.,Suffolk, P.M.,Vasudevan, S.G.,Dixon, N.E.,Ollis, D.L.
X-ray structure of the signal transduction protein from Escherichia coli at 1.9 A.
Acta Crystallogr.,Sect.D, 52:93-104, 1996

PubMed Abstract: 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.

PubMed: 15299730
DOI: 10.1107/S0907444995007293

Experimental method

X-RAY DIFFRACTION (1.9 Å)