1bym: Difference between revisions

Revision as of 19:57, 30 June 2008

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File:1bym.png

Template:STRUCTURE 1bym

SOLUTION STRUCTURES OF THE C-TERMINAL DOMAIN OF DIPHTHERIA TOXIN REPRESSORSOLUTION STRUCTURES OF THE C-TERMINAL DOMAIN OF DIPHTHERIA TOXIN REPRESSOR

Template:ABSTRACT PUBMED 10339551

About this StructureAbout this Structure

1BYM is a Single protein structure of sequence from Corynebacterium diphtheriae. Full experimental information is available from OCA.

ReferenceReference

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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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===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10339551}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10339551 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10339551}}
 ==About this Structure==
-BYM 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].
+BYM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYM OCA].
 ==Reference==
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 [[Category: Repressor]]
 [[Category: Transcription regulation]]
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