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Structure of the I1 early intermediate of photoactive yellow protein by FTIR spectroscopy.
Nat Struct Biol. 2001 Mar; 8(3):265-70.NS

Abstract

To understand how proteins translate the energy of sunlight into defined conformational changes, we have measured the photocycle reactions of photoactive yellow protein (PYP) using time-resolved step scan Fourier transform infrared (FTIR) spectroscopy. Global fit analysis yielded the same apparent time constants for the reactions of the chromophore, the protonation changes of protein side chains and the protein backbone motions, indicating that the light cycle reactions are synchronized. Changes in absorbance indicate that there are at least four intermediates (I1, I1', I2, I2'). In the intermediate I1, the dark-state hydrogen bond from Glu 46 to the aromatic ring of the p-hydroxycinnamoyl chromophore is preserved, implying that the chromophore undergoes trans to cis isomerization by flipping, not the aromatic ring, but the thioester linkage with the protein. This excludes an I1 structural model proposed on the basis of time resolved Laue crystallography, but does agree with the cryotrapped structure of an I1 precursor.

Authors+Show Affiliations

Brudler R
Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA. rbrudler@scripps.edu
Rammelsberg R
No affiliation info available
Woo TT
No affiliation info available
Getzoff ED
No affiliation info available
Gerwert K
No affiliation info available

MeSH

Amino Acid SubstitutionBacterial ProteinsBinding SitesColoring AgentsDarknessGlutamic AcidHalorhodospira halophilaHydrogen BondingInfrared RaysIsomerismKineticsLightModels, ChemicalModels, MolecularMutationPhotochemistryPhotoreceptors, MicrobialProtein ConformationSpectrophotometry, InfraredSpectroscopy, Fourier Transform InfraredSpectrum Analysis, RamanVibration

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

11224574

Citation

Brudler, R, et al. "Structure of the I1 Early Intermediate of Photoactive Yellow Protein By FTIR Spectroscopy." Nature Structural Biology, vol. 8, no. 3, 2001, pp. 265-70.
Brudler R, Rammelsberg R, Woo TT, et al. Structure of the I1 early intermediate of photoactive yellow protein by FTIR spectroscopy. Nat Struct Biol. 2001;8(3):265-70.
Brudler, R., Rammelsberg, R., Woo, T. T., Getzoff, E. D., & Gerwert, K. (2001). Structure of the I1 early intermediate of photoactive yellow protein by FTIR spectroscopy. Nature Structural Biology, 8(3), 265-70.
Brudler R, et al. Structure of the I1 Early Intermediate of Photoactive Yellow Protein By FTIR Spectroscopy. Nat Struct Biol. 2001;8(3):265-70. PubMed PMID: 11224574.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structure of the I1 early intermediate of photoactive yellow protein by FTIR spectroscopy. AU - Brudler,R, AU - Rammelsberg,R, AU - Woo,T T, AU - Getzoff,E D, AU - Gerwert,K, PY - 2001/2/27/pubmed PY - 2001/4/3/medline PY - 2001/2/27/entrez SP - 265 EP - 70 JF - Nature structural biology JO - Nat Struct Biol VL - 8 IS - 3 N2 - To understand how proteins translate the energy of sunlight into defined conformational changes, we have measured the photocycle reactions of photoactive yellow protein (PYP) using time-resolved step scan Fourier transform infrared (FTIR) spectroscopy. Global fit analysis yielded the same apparent time constants for the reactions of the chromophore, the protonation changes of protein side chains and the protein backbone motions, indicating that the light cycle reactions are synchronized. Changes in absorbance indicate that there are at least four intermediates (I1, I1', I2, I2'). In the intermediate I1, the dark-state hydrogen bond from Glu 46 to the aromatic ring of the p-hydroxycinnamoyl chromophore is preserved, implying that the chromophore undergoes trans to cis isomerization by flipping, not the aromatic ring, but the thioester linkage with the protein. This excludes an I1 structural model proposed on the basis of time resolved Laue crystallography, but does agree with the cryotrapped structure of an I1 precursor. SN - 1072-8368 UR - https://www.unboundmedicine.com/medline/citation/11224574/Structure_of_the_I1_early_intermediate_of_photoactive_yellow_protein_by_FTIR_spectroscopy_ DB - PRIME DP - Unbound Medicine ER -