3pyp
From Proteopedia
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|PDB= 3pyp |SIZE=350|CAPTION= <scene name='initialview01'>3pyp</scene>, resolution 0.85Å | |PDB= 3pyp |SIZE=350|CAPTION= <scene name='initialview01'>3pyp</scene>, resolution 0.85Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HC4:4'-HYDROXYCINNAMIC ACID'>HC4</scene> | + | |LIGAND= <scene name='pdbligand=HC4:4'-HYDROXYCINNAMIC+ACID'>HC4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3pyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pyp OCA], [http://www.ebi.ac.uk/pdbsum/3pyp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3pyp RCSB]</span> | ||
}} | }} | ||
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[[Category: Kuhn, P.]] | [[Category: Kuhn, P.]] | ||
[[Category: Soltis, S M.]] | [[Category: Soltis, S M.]] | ||
| - | [[Category: HC4]] | ||
[[Category: light sensor for negative phototaxis]] | [[Category: light sensor for negative phototaxis]] | ||
[[Category: photoreceptor]] | [[Category: photoreceptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:35:40 2008'' |
Revision as of 02:35, 31 March 2008
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| , resolution 0.85Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
3PYP is a Single protein structure of sequence from Halorhodospira halophila. Full crystallographic information is available from OCA.
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:9515969
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