PDBsum entry 2pii

Signal transduction protein

PDB id: 2pii

Contents

Protein chain

112 a.a.

Waters ×312

References listed in PDB file

Key reference

Title

X-Ray structure of the signal transduction protein from escherichia coli at 1.9 a.

Authors

P.D.Carr, E.Cheah, P.M.Suffolk, S.G.Vasudevan, N.E.Dixon, D.L.Ollis.

Ref.

Acta Crystallogr D Biol Crystallogr, 1996, 52, 93. [DOI no: 10.1107/S0907444995007293]

PubMed id

15299730

Note In the PDB file this reference is annotated as "TO BE PUBLISHED". The citation details given above were identified by an automated search of PubMed on title and author names, giving a percentage match of 90%.

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.

Figure 4.
Fig. 4. MOLSCRIPT (Kraulis. 1991) schematic diagrams of the Pll monomer. (a) Present 1.9 ~ model. (b) Former 2.7~ model.

Figure 6.
Fig. 6. Secondary structre and hydrogen bonding withn the Pit monomer. This diagram was prepared using the program HERA (Hutchinson & Thornton, 990).

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1996, 52, 93-0) copyright 1996.

Secondary reference #1

Title

Escherichia coli pii protein: purification, Crystallization and oligomeric structure.

Authors

S.G.Vasudevan, C.Gedye, N.E.Dixon, E.Cheah, P.D.Carr, P.M.Suffolk, P.D.Jeffrey, D.L.Ollis.

Ref.

FEBS Lett, 1994, 337, 255-258. [DOI no: 10.1016/0014-5793(94)80203-3]

PubMed id

8293810

Secondary reference #2

Title

Structure of the escherichia coli signal transducing protein pii.

Authors

E.Cheah, P.D.Carr, P.M.Suffolk, S.G.Vasudevan, N.E.Dixon, D.L.Ollis.

Ref.

Structure, 1994, 2, 981-990. [DOI no: 10.1016/S0969-2126(94)00100-6]

PubMed id

7866749

Figure 4.
Figure 4. . MOLSCRIPT [43] schematic diagram of a P[II] monomer showing residue Tyr51, the site of uridylylation during conditions of low cellular nitrogen. Figure 4. . MOLSCRIPT [[3]43] schematic diagram of a P[II] monomer showing residue Tyr51, the site of uridylylation during conditions of low cellular nitrogen.

Figure 9.
Figure 9. . 2F[o]–F[c] omit map calculated at 2.7 å resolution and contoured at 1.0σ. Residues 32–38 were omitted from the F[c] calculations. The omitted region is shown in white and the non-omitted regions in yellow. Figure 9. . 2F[o]–F[c] omit map calculated at 2.7 å resolution and contoured at 1.0σ. Residues 32–38 were omitted from the F[c] calculations. The omitted region is shown in white and the non-omitted regions in yellow.

The above figures are reproduced from the cited reference with permission from Cell Press