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Three-dimensional structure of a macromolecular assembly that regulates type III secretion in Yersinia pestis.
- F. Schubot, M. W. Jackson, +4 authors D. Waugh
- Biology, Medicine
- Journal of molecular biology
- 4 March 2005
Two crystal structures of YopN in complex with its heterodimeric secretion chaperone SycN-YscB and the co-regulatory protein TyeA, respectively are reported, which are possible to construct a credible theoretical model of the Yopn-Sycn-yscB-TyeA complex. Expand
Selection and characterization of Yersinia pestis YopN mutants that constitutively block Yop secretion
Results suggest that a C‐terminal domain of YopN complexed with TyeA blocks Yop secretion from a cytosolic, not an extracellular, location. Expand
Structural basis for the exocellulase activity of the cellobiohydrolase CbhA from Clostridium thermocellum.
The detailed analysis of these structures reveals that, while key catalytic residues and overall fold are conserved in this enzyme and those of other family 9 glycoside hydrolases, the active site of GH9_CbhA is blocked off after the -2 subsite, which explains the inability of the active sites of CbhA to accommodate a long cellulose chain and to cut it internally. Expand
Crystal structure of the transcription factor sc‐mtTFB offers insights into mitochondrial transcription
- F. Schubot, C. Chen, J. Rose, T. Dailey, H. Dailey, B. Wang
- Biology, Medicine
- Protein science : a publication of the Protein…
- 1 October 2001
It is proposed that the promoter specificity region is located on the mitochondrial RNA polymerase and that binding of sc‐mtTFB indirectly mediates interaction of the core enzyme with the promoter site. Expand
Interactions between immunoglobulin-like and catalytic modules in Clostridium thermocellum cellulosomal cellobiohydrolase CbhA.
- I. Kataeva, V. Uversky, +4 authors L. Ljungdahl
- Biology, Medicine
- Protein engineering, design & selection : PEDS
- 1 November 2004
The results indicate that inactivation of the GH9 module occurs as a result of multiple structural disturbances finally affecting the topology of the catalytic center. Expand
Structural basis for the substrate specificity of the feruloyl esterase domain of the cellulosomal xylanase Z from Clostridium thermocellum.
This work presents the crystal structure of FAE_XynZ, the domain of Clostridium thermocellum's cellulosomal xylanase Z that displays feruloyl esterase activity and defines the substrate specificity determinants of the enzyme. Expand
Structural Analysis of the Regulatory Domain of ExsA, a Key Transcriptional Regulator of the Type Three Secretion System in Pseudomonas aeruginosa
The crystal structure of the regulatory domain of ExsA, which is known to mediateexsA dimerization as well as ExsD binding, is reported and suggests two models for the Exs a dimer, which are supported by the observation that a mutation in α-2 greatly diminished the ability ofExsA to activate transcription in vitro. Expand
Structure of the POZ domain of human LRF, a master regulator of oncogenesis.
- F. Schubot, J. Tropea, D. Waugh
- Chemistry, Medicine
- Biochemical and biophysical research…
- 8 December 2006
The crystal structure of the LRF POZ domain reveals a high degree of structural conservation with the corresponding domains of BCL6 and PLZF, and the conservation of crystal packing contacts suggests the probable location of the interface that mediates LRF/BCL6 complex formation. Expand
Crystal structure and oligomeric state of the RetS signaling kinase sensory domain
The crystal structure of the RetS sensory domain is determined, and it is revealed that the sensory domain dimerizes with a dissociation constant of Kd = 580 ± 50 nM, a result with interesting implications for the understanding of the underlying signaling mechanism. Expand
Analysis of the crystal structure of the ExsC.ExsE complex reveals distinctive binding interactions of the Pseudomonas aeruginosa type III secretion chaperone ExsC with ExsE and ExsD.
The crystal structure of the T3SS chaperone ExsC in complex with its cognate effector ExsE has been determined and critical contacts that mediate the interactions between these two proteins are revealed. Expand