Structure and activity of tryptophan-rich TSPO proteins

Author:

Guo Youzhong1,Kalathur Ravi C.2,Liu Qun23,Kloss Brian2,Bruni Renato2,Ginter Christopher2,Kloppmann Edda24,Rost Burkhard24,Hendrickson Wayne A.1235

Affiliation:

1. Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.

2. The New York Consortium on Membrane Protein Structure (NYCOMPS), New York Structural Biology Center, 89 Convent Avenue, New York, NY 10027, USA.

3. New York Structural Biology Center, Synchrotron Beamlines, Brookhaven National Laboratory, Upton, NY 11973, USA.

4. Department of Informatics, Bioinformatics and Computational Biology, Technische Universität München, Garching 85748, Germany.

5. Department of Physiology and Cellular Biophysics, Columbia University, New York, NY 10032, USA.

Abstract

Structural clues to protein function Translocator protein (TSPO) is a mitochondrial membrane protein thought to transport cholesterol and porphyrins. Its detailed function remains unclear, but interest in it is high because TSPO is involved in a variety of human diseases. Two papers now present crystal structures of bacterial TSPOs. Li et al. show that a mutant that mimics a human single polymorphism associated with psychiatric disorders has structural changes in a region implicated in cholesterol binding. Guo et al. suggest that TSPO may be more than a transporter. They show how it catalyzes the degradation of porphyrins, a function that could be important in protection against oxidative stress. Science , this issue p. 555 , p. 551

Funder

NIH

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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