1bym: Difference between revisions
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'''SOLUTION STRUCTURES OF THE C-TERMINAL DOMAIN OF DIPHTHERIA TOXIN REPRESSOR''' | {{Structure | ||
|PDB= 1bym |SIZE=350|CAPTION= <scene name='initialview01'>1bym</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= DTXR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1717 Corynebacterium diphtheriae]) | |||
}} | |||
'''SOLUTION STRUCTURES OF THE C-TERMINAL DOMAIN OF DIPHTHERIA TOXIN REPRESSOR''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1BYM is a [ | 1BYM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYM OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10339551 10339551] | ||
[[Category: Corynebacterium diphtheriae]] | [[Category: Corynebacterium diphtheriae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:17:32 2008'' | ||
Revision as of 08:17, 20 March 2008
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| Gene: | DTXR (Corynebacterium diphtheriae) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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