3pyp: Difference between revisions

Revision as of 13:04, 3 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:3pyp.png

Template:STRUCTURE 3pyp

PHOTOACTIVE YELLOW PROTEIN, CRYOTRAPPED EARLY LIGHT CYCLE INTERMEDIATEPHOTOACTIVE YELLOW PROTEIN, CRYOTRAPPED EARLY LIGHT CYCLE INTERMEDIATE

Template:ABSTRACT PUBMED 9515969

About this StructureAbout this Structure

3PYP is a Single protein structure of sequence from Halorhodospira halophila. Full crystallographic information is available from OCA.

ReferenceReference

Structure at 0.85 A resolution of an early protein photocycle intermediate., Genick UK, Soltis SM, Kuhn P, Canestrelli IL, Getzoff ED, Nature. 1998 Mar 12;392(6672):206-9. PMID:9515969

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OCA

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-[[Image:3pyp.gif|left|200px]]
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 {{STRUCTURE_3pyp|  PDB=3pyp  |  SCENE=  }}
-'''PHOTOACTIVE YELLOW PROTEIN, CRYOTRAPPED EARLY LIGHT CYCLE INTERMEDIATE'''
+===PHOTOACTIVE YELLOW PROTEIN, CRYOTRAPPED EARLY LIGHT CYCLE INTERMEDIATE===
-==Overview==
+<!--
-Protein photosensors from all kingdoms of life use bound organic molecules, known as chromophores, to detect light. A specific double bond within each chromophore is isomerized by light, triggering slower changes in the protein as a whole. The initial movements of the chromophore, which can occur in femtoseconds, are tightly constrained by the surrounding protein, making it difficult to see how isomerization can occur, be recognized, and be appropriately converted into a protein-wide structural change and biological signal. Here we report how this dilemma is resolved in the photoactive yellow protein (PYP). We trapped a key early intermediate in the light cycle of PYP at temperatures below -100 degrees C, and determined its structure at better than 1 A resolution. The 4-hydroxycinnamoyl chromophore isomerizes by flipping its thioester linkage with the protein, thus avoiding collisions resulting from large-scale movement of its aromatic ring during the initial light reaction. A protein-to-chromophore hydrogen bond that is present in both the preceding dark state and the subsequent signalling state of the photosensor breaks, forcing one of the hydrogen-bonding partners into a hydrophobic pocket. The isomerized bond is distorted into a conformation resembling that in the transition state. The resultant stored energy is used to drive the PYP light cycle. These results suggest a model for phototransduction, with implications for bacteriorhodopsin, photoactive proteins, PAS domains, and signalling proteins.
+The line below this paragraph, {{ABSTRACT_PUBMED_9515969}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9515969 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9515969}}
 ==About this Structure==
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 [[Category: Light sensor for negative phototaxis]]
 [[Category: Photoreceptor]]
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