Structural and dynamic changes of photoactive yellow protein during its photocycle in solution

G Rubinstenn; G W Vuister; F A Mulder; P E Düx; R Boelens; K J Hellingwerf; R Kaptein

doi:10.1038/823

Structural and dynamic changes of photoactive yellow protein during its photocycle in solution

G Rubinstenn, G W Vuister, F A Mulder, P E Düx, R Boelens, K J Hellingwerf, R Kaptein

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

Light irradiation of photoactive yellow protein (PYP) induces a photocycle, in which red-shifted (pR) and blue-shifted (pB) intermediates have been characterized. An NMR study of the long-lived pB intermediate now reveals that it exhibits a large degree of disorder and exists as a family of multiple conformers that exchange on a millisecond time scale. This shows that the behavior of PYP in solution is different from what has been observed in the crystalline state. Furthermore, differential refolding to ground state pG is observed, whereby the central beta-sheet and parts of the helical structure are formed first and the region around the chromophore at a later stage.

Original language	English
Pages (from-to)	568-70
Number of pages	3
Journal	Nature Structural Biology
Volume	5
Issue number	7
DOIs	https://doi.org/10.1038/823
Publication status	Published - Jul 1998

Keywords

Bacterial Proteins
Chromatiaceae
Lasers
Nuclear Magnetic Resonance, Biomolecular
Photoreceptors, Microbial
Protein Conformation

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10.1038/823

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title = "Structural and dynamic changes of photoactive yellow protein during its photocycle in solution",

abstract = "Light irradiation of photoactive yellow protein (PYP) induces a photocycle, in which red-shifted (pR) and blue-shifted (pB) intermediates have been characterized. An NMR study of the long-lived pB intermediate now reveals that it exhibits a large degree of disorder and exists as a family of multiple conformers that exchange on a millisecond time scale. This shows that the behavior of PYP in solution is different from what has been observed in the crystalline state. Furthermore, differential refolding to ground state pG is observed, whereby the central beta-sheet and parts of the helical structure are formed first and the region around the chromophore at a later stage.",

keywords = "Bacterial Proteins, Chromatiaceae, Lasers, Nuclear Magnetic Resonance, Biomolecular, Photoreceptors, Microbial, Protein Conformation",

author = "G Rubinstenn and Vuister, {G W} and Mulder, {F A} and D{\"u}x, {P E} and R Boelens and Hellingwerf, {K J} and R Kaptein",

year = "1998",

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doi = "10.1038/823",

language = "English",

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journal = "Nature Structural Biology",

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T1 - Structural and dynamic changes of photoactive yellow protein during its photocycle in solution

AU - Rubinstenn, G

AU - Vuister, G W

AU - Mulder, F A

AU - Düx, P E

AU - Boelens, R

AU - Hellingwerf, K J

AU - Kaptein, R

PY - 1998/7

Y1 - 1998/7

N2 - Light irradiation of photoactive yellow protein (PYP) induces a photocycle, in which red-shifted (pR) and blue-shifted (pB) intermediates have been characterized. An NMR study of the long-lived pB intermediate now reveals that it exhibits a large degree of disorder and exists as a family of multiple conformers that exchange on a millisecond time scale. This shows that the behavior of PYP in solution is different from what has been observed in the crystalline state. Furthermore, differential refolding to ground state pG is observed, whereby the central beta-sheet and parts of the helical structure are formed first and the region around the chromophore at a later stage.

AB - Light irradiation of photoactive yellow protein (PYP) induces a photocycle, in which red-shifted (pR) and blue-shifted (pB) intermediates have been characterized. An NMR study of the long-lived pB intermediate now reveals that it exhibits a large degree of disorder and exists as a family of multiple conformers that exchange on a millisecond time scale. This shows that the behavior of PYP in solution is different from what has been observed in the crystalline state. Furthermore, differential refolding to ground state pG is observed, whereby the central beta-sheet and parts of the helical structure are formed first and the region around the chromophore at a later stage.

KW - Bacterial Proteins

KW - Chromatiaceae

KW - Lasers

KW - Nuclear Magnetic Resonance, Biomolecular

KW - Photoreceptors, Microbial

KW - Protein Conformation

U2 - 10.1038/823

DO - 10.1038/823

M3 - Article

C2 - 9665170

SN - 1072-8368

VL - 5

SP - 568

EP - 570

JO - Nature Structural Biology

JF - Nature Structural Biology

IS - 7

ER -

Structural and dynamic changes of photoactive yellow protein during its photocycle in solution

Abstract

Keywords

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