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Conformational substates in different crystal forms of the photoactive yellow protein—Correlation with theoretical and experimental flexibility

Published online by Cambridge University Press:  01 January 2000

DAAN M.F. VAN AALTEN
Affiliation:
W.M. Keck Structural Biology, Cold Spring Harbor Laboratory, 1 Bungtown Road, Cold Spring Harbor, New York 11724 Current address: Department of Biochemistry, Wellcome Trust Biocentre, Dow Street, University of Dundee, Dundee, DD1 SEH Scotland, UK.
WIM CRIELAARD
Affiliation:
Department of Microbiology, E.C. Slater Institute, BioCentrum, University of Amsterdam, The Netherlands
KLAAS J. HELLINGWERF
Affiliation:
Department of Microbiology, E.C. Slater Institute, BioCentrum, University of Amsterdam, The Netherlands
LEEMOR JOSHUA-TOR
Affiliation:
W.M. Keck Structural Biology, Cold Spring Harbor Laboratory, 1 Bungtown Road, Cold Spring Harbor, New York 11724
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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.

Type
Research Article
Copyright
© 2000 The Protein Society

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