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2ZOI

Neutron Crystal Structure of Photoactive Yellow Protein, Wild type, at 295K

Summary for 2ZOI
Entry DOI10.2210/pdb2zoi/pdb
Related2ZOH
DescriptorPhotoactive yellow protein, 4'-HYDROXYCINNAMIC ACID (3 entities in total)
Functional Keywordspas, lov, photoreceptor, light sensor, lbhb, shb, chromophore, photoreceptor protein, receptor, sensory transduction, signaling protein
Biological sourceHalorhodospira halophila
Total number of polymer chains1
Total formula weight14052.73
Authors
Yamaguchi, S. (deposition date: 2008-05-21, release date: 2009-03-24, Last modification date: 2023-11-01)
Primary citationYamaguchi, S.,Kamikubo, H.,Kurihara, K.,Kuroki, R.,Niimura, N.,Shimizu, N.,Yamazaki, Y.,Kataoka, M.
Low-barrier hydrogen bond in photoactive yellow protein
Proc.Natl.Acad.Sci.USA, 106:440-444, 2009
Cited by
PubMed Abstract: Low-barrier hydrogen bonds (LBHBs) have been proposed to play roles in protein functions, including enzymatic catalysis and proton transfer. Transient formation of LBHBs is expected to stabilize specific reaction intermediates. However, based on experimental results and theoretical considerations, arguments against the importance of LBHB in proteins have been raised. The discrepancy is caused by the absence of direct identification of the hydrogen atom position. Here, we show by high-resolution neutron crystallography of photoactive yellow protein (PYP) that a LBHB exists in a protein, even in the ground state. We identified approximately 87% (819/942) of the hydrogen positions in PYP and demonstrated that the hydrogen bond between the chromophore and E46 is a LBHB. This LBHB stabilizes an isolated electric charge buried in the hydrophobic environment of the protein interior. We propose that in the excited state the fast relaxation of the LBHB into a normal hydrogen bond is the trigger for photo-signal propagation to the protein moiety. These results give insights into the novel roles of LBHBs and the mechanism of the formation of LBHBs.
PubMed: 19122140
DOI: 10.1073/pnas.0811882106
PDB entries with the same primary citation
Experimental method
NEUTRON DIFFRACTION (1.5 Å)
Structure validation

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