Global conformational changes control the reactivity of methane monooxygenase

S. Gallagher, Anastasia Callaghan, J. Zhao, H. Dalton, J. Trewhella

Research output: Contribution to journalArticlepeer-review


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.
Original languageEnglish
Pages (from-to)6752-6760
Number of pages9
Issue number21
Publication statusPublished - 1999


Dive into the research topics of 'Global conformational changes control the reactivity of methane monooxygenase'. Together they form a unique fingerprint.

Cite this