2bun: Difference between revisions

Revision as of 18:56, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2bun.png

Template:STRUCTURE 2bun

SOLUTION STRUCTURE OF THE BLUF DOMAIN OF APPA 5-125SOLUTION STRUCTURE OF THE BLUF DOMAIN OF APPA 5-125

Template:ABSTRACT PUBMED 16323221

About this StructureAbout this Structure

2BUN is a Single protein structure of sequence from Rhodobacter sphaeroides. Full experimental information is available from OCA.

ReferenceReference

The solution structure of the AppA BLUF domain: insight into the mechanism of light-induced signaling., Grinstead JS, Hsu ST, Laan W, Bonvin AM, Hellingwerf KJ, Boelens R, Kaptein R, Chembiochem. 2006 Jan;7(1):187-93. PMID:16323221

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

OCA

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-'''SOLUTION STRUCTURE OF THE BLUF DOMAIN OF APPA 5-125'''
+===SOLUTION STRUCTURE OF THE BLUF DOMAIN OF APPA 5-125===
-==Overview==
+<!--
-The transcriptional antirepressor AppA from the photosynthetic bacterium Rhodobacter sphaeroides senses both the light climate and the intracellular redox state. Under aerobic conditions in the dark, AppA binds to and thereby blocks the function of PpsR, a transcriptional repressor. Absorption of a blue photon dissociates AppA from PpsR and allows the latter to repress photosynthesis gene expression. The N terminus of AppA contains sequence homology to flavin-containing photoreceptors that belong to the BLUF family. Structural and chemical aspects of signal transduction mediated by AppA are still largely unknown. Here we present NMR studies of the N-terminal flavin-binding BLUF domain of AppA. Its solution structure adopts an alpha/beta-sandwich fold with a beta alpha beta beta alpha beta beta topology, which represents a new flavin-binding fold. Considerable disorder is observed for residues near the chromophore due to conformational exchange. This disorder is observed both in the dark and in the light-induced signaling state of AppA. Furthermore, we detect light-induced structural changes in a patch of surface residues that provide a structural link between light absorption and signal-transduction events.
+The line below this paragraph, {{ABSTRACT_PUBMED_16323221}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16323221 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16323221}}
 ==About this Structure==
-BUN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUN OCA].
+BUN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUN OCA].
 ==Reference==
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 [[Category: Bluf domain]]
 [[Category: Fad]]
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