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Journal Article

Functional (un)cooperativity in elevator transport proteins.


Geertsma,  Eric R
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Holzhüter, K., & Geertsma, E. R. (2020). Functional (un)cooperativity in elevator transport proteins. Biochemical Society transactions, 48(3), 1047-1055. doi:10.1042/BST20190970.

Cite as: https://hdl.handle.net/21.11116/0000-0008-A2B0-9
The activity of enzymes is subject to regulation at multiple levels. Cooperativity, the interconnected behavior of active sites within a protein complex, directly affects protein activity. Cooperativity is a mode of regulation that requires neither extrinsic factors nor protein modifications. Instead, it allows enzymes themselves to modulate reaction rates. Cooperativity is an important regulatory mechanism in soluble proteins, but also examples of cooperative membrane proteins have been described. In this review, we summarize the current knowledge on interprotomer cooperativity in elevator-type proteins, a class of membrane transporters characterized by large rigid-body movements perpendicular to the membrane, and highlight well-studied examples and experimental approaches.