PDBsum entry: 1dz3

Response regulator

PDB id: 1dz3

Contents

Protein chain

123 a.a. *

Ligands

SO4

Waters ×95

* Residue conservation analysis

PDB id:

1dz3

Name:

Response regulator

Title:

Domain-swapping in the sporulation response regulator spo0a

Structure:

Stage 0 sporulation protein a. Chain: a. Fragment: receiver domain. Engineered: yes

Source:

Bacillus stearothermophilus. Organism_taxid: 1422. Cellular_location: cytoplasm. Gene: spo0a. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PDB file)

Resolution:

1.65Å R-factor: 0.235 R-free: 0.265

Authors:

R.J.Lewis,J.A.Brannigan,K.Muchova,G.Leonard,I.Barak, A.J.Wilkinson

Key ref:

R.J.Lewis et al. (2000). Domain swapping in the sporulation response regulator Spo0A. J Mol Biol, 297, 757-770. PubMed id: 10731426 DOI: 10.1006/jmbi.2000.3598

Date:

15-Feb-00 Release date: 10-Apr-00

Protein chain

P52934  (SP0A_GEOSE) -  Stage 0 sporulation protein A

Seq: 259 a.a.

Struc: 123 a.a.

 Gene Ontology (GO) functional annotation 

• Biological process: two-component signal transduction system (phosphorelay) (4 terms)
• Biochemical function: two-component response regulator activity (3 terms)

DOI no: 10.1006/jmbi.2000.3598

J Mol Biol 297:757-770 (2000)

PubMed id: 10731426

Domain swapping in the sporulation response regulator Spo0A.

R.J.Lewis, K.Muchová, J.A.Brannigan, I.Barák, G.Leonard, A.J.Wilkinson.

ABSTRACT

Adaptive responses of micro-organisms, such as chemotaxis and sporulation, are governed by two-component systems consisting of sensor kinases, that interpret environmental signals, and response regulators which activate the appropriate physiological responses. Signal transduction via response regulator proteins is mediated through transient phosphorylation of aspartic acid residues. In Spo0A, the key regulator of development (sporulation) in Bacillus, phosphorylation of the N-terminal receiver domain (N-Spo0A) at aspartate-55 switches on the transcription activation functions residing in the C-terminal effector domain. Here we report the crystal structure of N-Spo0A from Bacillus stearothermophilus at 1.6 A spacing, revealing a dimer formed by an alpha-helix swap. Comparison of this structure with the recently described structure of phosphorylated N-Spo0A shows that dimer formation results from a cis-trans isomerization of the Lys106--Pro107 peptide bond. The quaternary reorganization is associated with alterations in the active site stereochemistry which may have implications for signalling. Remarkably, this 3-D domain swapped N-Spo0A dimer has an identical topology to a hypothetical CheY-like dimer, recently proposed as an intermediate in the evolution of the family of periplasmic substrate binding proteins.

Selected figure(s)

Figure 2.
Figure 2. (a) Ribbon and (b) space filling representations of the N-Spo0A dimer. One protomer is coloured red, the other green. The side-chains of Lys106 and Asp55 are in dark blue.

Figure 3.
Figure 3. Stereo view of a comparative C^a trace of the N-Spo0A vert, similar P monomeric structure coloured in blue and the N-Spo0A dimer coloured in green for molecule 1 (residues 2-108) and red for molecule 2 (helix a5, residues 108-122). The view is looking down onto the active site with the aspartyl-phosphate and the calcium ion of N-Spo0A vert, similar P drawn as ball-and-stick models. The structures were superimposed by least-squares minimization procedures applied to the C^a atoms of residues 2-100 of molecule 1 and 112-123 of molecule 2 from N-Spo0A, and residues 2-100 and 112-123 from one molecule of N-Spo0A vert, similar P.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2000, 297, 757-770) copyright 2000.

Figures were selected by an automated process.