1bym
From Proteopedia
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'''SOLUTION STRUCTURES OF THE C-TERMINAL DOMAIN OF DIPHTHERIA TOXIN REPRESSOR''' | '''SOLUTION STRUCTURES OF THE C-TERMINAL DOMAIN OF DIPHTHERIA TOXIN REPRESSOR''' | ||
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[[Category: Wang, G.]] | [[Category: Wang, G.]] | ||
[[Category: Wylie, G P.]] | [[Category: Wylie, G P.]] | ||
| - | [[Category: | + | [[Category: C-terminal domain]] |
| - | [[Category: | + | [[Category: Dtxr]] |
| - | [[Category: | + | [[Category: Peptide-binding]] |
| - | [[Category: | + | [[Category: Prokaryotic sh3 domain]] |
| - | [[Category: | + | [[Category: Repressor]] |
| - | [[Category: | + | [[Category: Transcription regulation]] |
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Revision as of 09:07, 2 May 2008
SOLUTION STRUCTURES OF THE C-TERMINAL DOMAIN OF DIPHTHERIA TOXIN REPRESSOR
Overview
The diphtheria toxin repressor (DtxR) is the best-characterized member of a family of homologous proteins that regulate iron uptake and virulence gene expression in the Gram-positive bacteria. DtxR contains two domains that are separated by a short, unstructured linker. The N-terminal domain is structurally well-defined and is responsible for Fe2+ binding, dimerization, and DNA binding. The C-terminal domain adopts a fold similar to eukaryotic Src homology 3 domains, but the functional role of the C-terminal domain in repressor activity is unknown. The solution structure of the C-terminal domain, consisting of residues N130-L226 plus a 13-residue N-terminal extension, has been determined by using NMR spectroscopy. Residues before A147 are highly mobile and adopt a random coil conformation, but residues A147-L226 form a single structured domain consisting of five beta-strands and three helices arranged into a partially orthogonal, two-sheet beta-barrel, similar to the structure observed in the crystalline Co2+ complex of full-length DtxR. Chemical shift perturbation studies demonstrate that a proline-rich peptide corresponding to residues R125-G139 of intact DtxR binds to the C-terminal domain in a pocket formed by residues in beta-strands 2, 3, and 5, and helix 3. Binding of the proline-rich peptide by the C-terminal domain of DtxR presents an example of peptide binding by a prokaryotic Src homology 3-like protein. The results of this study, combined with previous x-ray studies of intact DtxR, provide insights into a possible biological function of the C-terminal domain in regulating repressor activity.
About this Structure
1BYM is a Single protein structure of sequence from Corynebacterium diphtheriae. Full crystallographic information is available from OCA.
Reference
Solution structure and peptide binding studies of the C-terminal src homology 3-like domain of the diphtheria toxin repressor protein., Wang G, Wylie GP, Twigg PD, Caspar DL, Murphy JR, Logan TM, Proc Natl Acad Sci U S A. 1999 May 25;96(11):6119-24. PMID:10339551 Page seeded by OCA on Fri May 2 12:07:21 2008
