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Global conformational changes control the reactivity of methane monooxygenase

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Global conformational changes control the reactivity of methane monooxygenase. / Gallagher, S.; Callaghan, Anastasia; Zhao, J.; Dalton, H.; Trewhella, J.

In: Biochemistry, Vol. 38, No. 21, 1999, p. 6752-6760.

Research output: Contribution to journalArticlepeer-review

Harvard

Gallagher, S, Callaghan, A, Zhao, J, Dalton, H & Trewhella, J 1999, 'Global conformational changes control the reactivity of methane monooxygenase', Biochemistry, vol. 38, no. 21, pp. 6752-6760. https://doi.org/10.1021/bi982991n

APA

Gallagher, S., Callaghan, A., Zhao, J., Dalton, H., & Trewhella, J. (1999). Global conformational changes control the reactivity of methane monooxygenase. Biochemistry, 38(21), 6752-6760. https://doi.org/10.1021/bi982991n

Vancouver

Gallagher S, Callaghan A, Zhao J, Dalton H, Trewhella J. Global conformational changes control the reactivity of methane monooxygenase. Biochemistry. 1999;38(21):6752-6760. https://doi.org/10.1021/bi982991n

Author

Gallagher, S. ; Callaghan, Anastasia ; Zhao, J. ; Dalton, H. ; Trewhella, J. / Global conformational changes control the reactivity of methane monooxygenase. In: Biochemistry. 1999 ; Vol. 38, No. 21. pp. 6752-6760.

Bibtex

@article{020681f57f2a4c6f8e3beb602a2429d6,
title = "Global conformational changes control the reactivity of methane monooxygenase",
abstract = "We present here X-ray scattering data that yield new structural information on the multicomponent enzyme methane monooxygenase and its components:  a hydroxylase dimer, and two copies each of a reductase and regulatory protein B. Upon formation of the enzyme complex, the hydroxylase undergoes a dramatic conformational change that is observed in the scattering data as a fundamental change in shape of the scattering particle such that one dimension is narrowed (by 25% or 24 {\AA}) while the longest dimension increases (by 20% or 25 {\AA}). These changes also are reflected in a 13% increase in radius of gyration upon complex formation. Both the reductase and protein B are required for inducing the conformational change. We have modeled the scattering data for the complex by systematically modifying the crystal structure of the hydroxylase and using ellipsoids to represent the reductase and protein B components. Our model indicates that protein B plays a role in optimizing the interaction between the active centers of the reductase and hydroxylase components, thus, facilitating electron transfer between them. In addition, the model suggests reasons why the hydroxylase exists as a dimer and that a possible role for the outlying γ-subunit may be to stabilize the complex through its interaction with the other components. We further show that proteolysis of protein B to form the inactive B{\textquoteleft} results in a conformational change and B{\textquoteleft} does not bind to the hydroxylase. The truncation thus could represent a regulatory mechanism for controlling the enzyme activity.",
author = "S. Gallagher and Anastasia Callaghan and J. Zhao and H. Dalton and J. Trewhella",
year = "1999",
doi = "10.1021/bi982991n",
language = "English",
volume = "38",
pages = "6752--6760",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "21",

}

RIS

TY - JOUR

T1 - Global conformational changes control the reactivity of methane monooxygenase

AU - Gallagher, S.

AU - Callaghan, Anastasia

AU - Zhao, J.

AU - Dalton, H.

AU - Trewhella, J.

PY - 1999

Y1 - 1999

N2 - We present here X-ray scattering data that yield new structural information on the multicomponent enzyme methane monooxygenase and its components:  a hydroxylase dimer, and two copies each of a reductase and regulatory protein B. Upon formation of the enzyme complex, the hydroxylase undergoes a dramatic conformational change that is observed in the scattering data as a fundamental change in shape of the scattering particle such that one dimension is narrowed (by 25% or 24 Å) while the longest dimension increases (by 20% or 25 Å). These changes also are reflected in a 13% increase in radius of gyration upon complex formation. Both the reductase and protein B are required for inducing the conformational change. We have modeled the scattering data for the complex by systematically modifying the crystal structure of the hydroxylase and using ellipsoids to represent the reductase and protein B components. Our model indicates that protein B plays a role in optimizing the interaction between the active centers of the reductase and hydroxylase components, thus, facilitating electron transfer between them. In addition, the model suggests reasons why the hydroxylase exists as a dimer and that a possible role for the outlying γ-subunit may be to stabilize the complex through its interaction with the other components. We further show that proteolysis of protein B to form the inactive B‘ results in a conformational change and B‘ does not bind to the hydroxylase. The truncation thus could represent a regulatory mechanism for controlling the enzyme activity.

AB - We present here X-ray scattering data that yield new structural information on the multicomponent enzyme methane monooxygenase and its components:  a hydroxylase dimer, and two copies each of a reductase and regulatory protein B. Upon formation of the enzyme complex, the hydroxylase undergoes a dramatic conformational change that is observed in the scattering data as a fundamental change in shape of the scattering particle such that one dimension is narrowed (by 25% or 24 Å) while the longest dimension increases (by 20% or 25 Å). These changes also are reflected in a 13% increase in radius of gyration upon complex formation. Both the reductase and protein B are required for inducing the conformational change. We have modeled the scattering data for the complex by systematically modifying the crystal structure of the hydroxylase and using ellipsoids to represent the reductase and protein B components. Our model indicates that protein B plays a role in optimizing the interaction between the active centers of the reductase and hydroxylase components, thus, facilitating electron transfer between them. In addition, the model suggests reasons why the hydroxylase exists as a dimer and that a possible role for the outlying γ-subunit may be to stabilize the complex through its interaction with the other components. We further show that proteolysis of protein B to form the inactive B‘ results in a conformational change and B‘ does not bind to the hydroxylase. The truncation thus could represent a regulatory mechanism for controlling the enzyme activity.

U2 - 10.1021/bi982991n

DO - 10.1021/bi982991n

M3 - Article

VL - 38

SP - 6752

EP - 6760

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 21

ER -

ID: 158584