3pyp: Difference between revisions
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[[Image:3pyp.gif|left|200px]] | [[Image:3pyp.gif|left|200px]] | ||
'''PHOTOACTIVE YELLOW PROTEIN, CRYOTRAPPED EARLY LIGHT CYCLE INTERMEDIATE''' | {{Structure | ||
|PDB= 3pyp |SIZE=350|CAPTION= <scene name='initialview01'>3pyp</scene>, resolution 0.85Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=HC4:4'-HYDROXYCINNAMIC ACID'>HC4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''PHOTOACTIVE YELLOW PROTEIN, CRYOTRAPPED EARLY LIGHT CYCLE INTERMEDIATE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
3PYP is a [ | 3PYP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Halorhodospira_halophila Halorhodospira halophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PYP OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9515969 9515969] | ||
[[Category: Halorhodospira halophila]] | [[Category: Halorhodospira halophila]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: photoreceptor]] | [[Category: photoreceptor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:06:56 2008'' | ||
Revision as of 20:06, 20 March 2008
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PHOTOACTIVE YELLOW PROTEIN, CRYOTRAPPED EARLY LIGHT CYCLE INTERMEDIATE
OverviewOverview
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.
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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