1d7e: Difference between revisions

Revision as of 22:36, 30 June 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:1d7e.png

Template:STRUCTURE 1d7e

CRYSTAL STRUCTURE OF THE P65 CRYSTAL FORM OF PHOTOACTIVE YELLOW PROTEINCRYSTAL STRUCTURE OF THE P65 CRYSTAL FORM OF PHOTOACTIVE YELLOW PROTEIN

Template:ABSTRACT PUBMED 10739248

About this StructureAbout this Structure

1D7E is a Single protein structure of sequence from Halorhodospira halophila. Full crystallographic information is available from OCA.

ReferenceReference

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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OCA

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-'''CRYSTAL STRUCTURE OF THE P65 CRYSTAL FORM OF PHOTOACTIVE YELLOW PROTEIN'''
+===CRYSTAL STRUCTURE OF THE P65 CRYSTAL FORM OF PHOTOACTIVE YELLOW PROTEIN===
-==Overview==
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-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.
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 [[Category: Joshua-Tor, L.]]
 [[Category: Photoreceptor]]
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