1d7e
From Proteopedia
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|PDB= 1d7e |SIZE=350|CAPTION= <scene name='initialview01'>1d7e</scene>, resolution 1.39Å | |PDB= 1d7e |SIZE=350|CAPTION= <scene name='initialview01'>1d7e</scene>, resolution 1.39Å | ||
|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=[[2phy|2PHY]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d7e OCA], [http://www.ebi.ac.uk/pdbsum/1d7e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d7e RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Hellingwerf, K J.]] | [[Category: Hellingwerf, K J.]] | ||
[[Category: Joshua-Tor, L.]] | [[Category: Joshua-Tor, L.]] | ||
| - | [[Category: HC4]] | ||
[[Category: photoreceptor]] | [[Category: photoreceptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:36:03 2008'' |
Revision as of 16:36, 30 March 2008
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| , resolution 1.39Å | |||||||
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| Ligands: | |||||||
| Related: | 2PHY
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE P65 CRYSTAL FORM OF PHOTOACTIVE YELLOW PROTEIN
Overview
The conformational changes during the photocycle of the photoactive yellow protein have been the subject of many recent studies. Spectroscopic measurements have shown that the photocycle also occurs in a crystalline environment, and this has been the basis for subsequent Laue diffraction and cryocrystallographic studies. These studies have shown that conformational changes during the photocycle are limited to the chromophore and its immediate environment. However, spectroscopic studies suggest the presence of large conformational changes in the protein. Here, we address this apparent discrepancy in two ways. First, we obtain a description of large concerted motions in the ground state of the yellow protein from NMR data and theoretical calculations. Second, we describe the high-resolution structure of the yellow protein crystallized in a different space group. The structure of the yellow protein differs significantly between the two crystal forms. We show that these differences can be used to obtain a description of the flexibility of the protein that is consistent with the motions observed in solution.
About this Structure
1D7E is a Single protein structure of sequence from Halorhodospira halophila. Full crystallographic information is available from OCA.
Reference
Conformational substates in different crystal forms of the photoactive yellow protein--correlation with theoretical and experimental flexibility., van Aalten DM, Crielaard W, Hellingwerf KJ, Joshua-Tor L, Protein Sci. 2000 Jan;9(1):64-72. PMID:10739248
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