1z3e: Difference between revisions

Revision as of 19:53, 28 July 2008

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File:1z3e.png

Template:STRUCTURE 1z3e

Crystal Structure of Spx in Complex with the C-terminal Domain of the RNA Polymerase Alpha SubunitCrystal Structure of Spx in Complex with the C-terminal Domain of the RNA Polymerase Alpha Subunit

Template:ABSTRACT PUBMED 16249335

About this StructureAbout this Structure

1Z3E is a Protein complex structure of sequences from Bacillus subtilis. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the Bacillus subtilis anti-alpha, global transcriptional regulator, Spx, in complex with the alpha C-terminal domain of RNA polymerase., Newberry KJ, Nakano S, Zuber P, Brennan RG, Proc Natl Acad Sci U S A. 2005 Nov 1;102(44):15839-44. Epub 2005 Oct 25. PMID:16249335

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OCA

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-'''Crystal Structure of Spx in Complex with the C-terminal Domain of the RNA Polymerase Alpha Subunit'''
+===Crystal Structure of Spx in Complex with the C-terminal Domain of the RNA Polymerase Alpha Subunit===
-==Overview==
+<!--
-Spx, a global transcription regulator in Bacillus subtilis, interacts with the C-terminal domain of the alpha subunit (alphaCTD) of RNA polymerase to control gene expression under conditions of disulfide stress, which is sensed by disulfide bond formation between Spx residues C10 and C13. Here, we describe the crystal structure of the B. subtilis alphaCTD bound to oxidized Spx. Analysis of the complex reveals interactions between three regions of "anti-alpha" Spx and helix alpha1 and the "261" determinant of alphaCTD. The former contact could disrupt the interaction between alphaCTD and activator proteins or alter the DNA-bound conformation of alphaCTD, thereby repressing activator-stimulated transcription. Binding to the 261 determinant would prevent interaction between alphaCTD and region 4 of sigma(A). Intriguingly, the Spx disulfide bond is far from the alphaCTD-Spx interface, suggesting that Spx regulates transcription allosterically or through the redox-dependent creation or destruction of binding sites for additional components of the transcription machinery.
+The line below this paragraph, {{ABSTRACT_PUBMED_16249335}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16249335 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16249335}}
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 [[Category: Bacterial transcription regulation]]
 [[Category: Disulfide stress]]
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