PDBsum entry 2oqr

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Transcription,signaling protein PDB id
Jmol PyMol
Protein chain
226 a.a. *
ACT ×2
_LA ×5
Waters ×163
* Residue conservation analysis
PDB id:
Name: Transcription,signaling protein
Title: The structure of the response regulator regx3 from mycobacte tuberculosis
Structure: Sensory transduction protein regx3. Chain: a. Engineered: yes
Source: Mycobacterium tuberculosis h37rv. Organism_taxid: 83332. Strain: h37rv. Gene: regx3. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.03Å     R-factor:   0.179     R-free:   0.217
Authors: J.King-Scott
Key ref:
J.King-Scott et al. (2007). The structure of a full-length response regulator from Mycobacterium tuberculosis in a stabilized three-dimensional domain-swapped, activated state. J Biol Chem, 282, 37717-37729. PubMed id: 17942407 DOI: 10.1074/jbc.M705081200
01-Feb-07     Release date:   16-Oct-07    
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Protein chain
P9WGL9  (REGX3_MYCTU) -  Sensory transduction protein regX3
227 a.a.
226 a.a.*
Key:    Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     intracellular   1 term 
  Biological process     regulation of response to stress   7 terms 
  Biochemical function     DNA binding     1 term  


DOI no: 10.1074/jbc.M705081200 J Biol Chem 282:37717-37729 (2007)
PubMed id: 17942407  
The structure of a full-length response regulator from Mycobacterium tuberculosis in a stabilized three-dimensional domain-swapped, activated state.
J.King-Scott, E.Nowak, E.Mylonas, S.Panjikar, M.Roessle, D.I.Svergun, P.A.Tucker.
The full-length, two-domain response regulator RegX3 from Mycobacterium tuberculosis is a dimer stabilized by three-dimensional domain swapping. Dimerization is known to occur in the OmpR/PhoB subfamily of response regulators upon activation but has previously only been structurally characterized for isolated receiver domains. The RegX3 dimer has a bipartite intermolecular interface, which buries 2357 A(2) per monomer. The two parts of the interface are between the two receiver domains (dimerization interface) and between a composite receiver domain and the effector domain of the second molecule (interdomain interface). The structure provides support for the importance of threonine and tyrosine residues in the signal transduction mechanism. These residues occur in an active-like conformation stabilized by lanthanum ions. In solution, RegX3 exists as both a monomer and a dimer in a concentration-dependent equilibrium. The dimer in solution differs from the active form observed in the crystal, resembling instead the model of the inactive full-length response regulator PhoB.
  Selected figure(s)  
Figure 1.
FIGURE 1. The full-length RR, RegX3, represented by the C[ ]trace of the single polypeptide chain in the asymmetric unit (ASU). Every 10th residue is labeled. Five La^3+ ions appear in the asymmetric unit and are colored magenta. The main C[ ]chain is colored from blue to red going from the N to C terminus.
Figure 7.
FIGURE 7. A stereo schematic diagram comparing the functional units from the open (A) and closed (B) subclasses of RRs superimposed via the receiver domain on to RegX3 (blue, 1-80 from the domain-swapped element; red, 81-226 from the functional unit). A, both DrrD (green; Protein Data Bank code 1KGS) and DrrB (yellow; Protein Data Bank code 1P2F) superimpose well onto the RegX3 composite receiver domain. The interdomain interface is mediated by 5 in RegX3 and DrrD but not in DrrB. The orientation of the effector domain in RegX3 differs from previously characterized full-length RRs of the OmpR/PhoB subfamily. The β-scaffold in DrrD and DrrB are positioned at the interdomain interface. B, as with the open class, the RegX3 composite receiver domain superimposes well onto the receiver domains of PrrA (magenta; Protein Data Bank code 1YS6) and MtrA (orange; Protein Data Bank code 2GWR). However, the orientation of the effector domain relative to the receiver domain is different in each case. The interdomain interface, in all closed subclasses, is mediated by 4, β5, and 5.
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2007, 282, 37717-37729) copyright 2007.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20080056 R.Gao, and A.M.Stock (2010).
Molecular strategies for phosphorylation-mediated regulation of response regulator activity.
  Curr Opin Microbiol, 13, 160-167.  
18798569 C.Meesters, A.Brack, N.Hellmann, and H.Decker (2009).
Structural characterization of the alpha-hemolysin monomer from Staphylococcus aureus.
  Proteins, 75, 118-126.  
18195018 J.E.Rhee, W.Sheng, L.K.Morgan, R.Nolet, X.Liao, and L.J.Kenney (2008).
Amino acids important for DNA recognition by the response regulator OmpR.
  J Biol Chem, 283, 8664-8677.  
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