1D7E

CRYSTAL STRUCTURE OF THE P65 CRYSTAL FORM OF PHOTOACTIVE YELLOW PROTEIN

Summary for 1D7E

• Entry DOI: 10.2210/pdb1d7e/pdb
• Related: 2PHY
• Descriptor: PHOTOACTIVE YELLOW PROTEIN, 4'-HYDROXYCINNAMIC ACID (3 entities in total)
• Functional Keywords: photoreceptor, photosynthesis
• Biological source: Halorhodospira halophila
• Total number of polymer chains: 1
• Total formula weight: 13654.28

Authors

Van Aalten, D.M.F.,Crielaard, W.,Hellingwerf, K.J.,Joshua-Tor, L. (deposition date: 1999-10-17, release date: 2000-03-31, Last modification date: 2018-01-31)

Primary citation

van Aalten, D.M.,Crielaard, W.,Hellingwerf, K.J.,Joshua-Tor, L.
Conformational substates in different crystal forms of the photoactive yellow protein--correlation with theoretical and experimental flexibility.
Protein Sci., 9:64-72, 2000

PubMed Abstract: 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.

PubMed: 10739248

Experimental method

X-RAY DIFFRACTION (1.39 Å)