View source for 1bym

[[Image:1bym.jpg|left|200px]]<br /><applet load="1bym" size="450" color="white" frame="true" align="right" spinBox="true" 
caption="1bym" />
'''SOLUTION STRUCTURES OF THE C-TERMINAL DOMAIN OF DIPHTHERIA TOXIN REPRESSOR'''<br />

==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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BYM 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10339551 10339551]
[[Category: Corynebacterium diphtheriae]]
[[Category: Single protein]]
[[Category: Caspar, D.L.D.]]
[[Category: Logan, T.M.]]
[[Category: Murphy, J.R.]]
[[Category: Twigg, P.D.]]
[[Category: Wang, G.]]
[[Category: Wylie, G.P.]]
[[Category: c-terminal domain]]
[[Category: dtxr]]
[[Category: peptide-binding]]
[[Category: prokaryotic sh3 domain]]
[[Category: repressor]]
[[Category: transcription regulation]]

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:01:54 2007''