Structure and activity of tryptophan-rich TSPO proteins
Open accessAbstract
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
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TSPO is predominantly α-helical, containing five helices clustered into a barrel-like shape.
“Biochemical evidence and recent structural determinations of the TSPO protein indicate that TSPO is predominantly α-helical, containing five helices clustered into a barrel-like shape (113–115).”
From Adrenal Mitochondria and Steroidogenesis: From Individual Proteins to Functional Protein Assemblies (2016) · cites this paper as [115]
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- Authors
- Guo, Y., Kalathur, R. C., Liu, Q., Kloss, B., Bruni, R., Ginter, C., Kloppmann, E., Rost, B., & Hendrickson, W. A.
- Affiliations
- Columbia University (US)
- New York Structural Biology Center (US)
- Brookhaven National Laboratory (US)
- Corresponding author
- Hendrickson, Wayne A.
- ORCID
- Venue
- Science
- Published
- 2015-01-30
- Volume
- 347
- Issue
- 6221
- Pages
- 551-555
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC4341906
- OpenAlex
- W1900110634
- Cited by
- 171
- References
- 0
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 15 · 2023: 10 · 2022: 10 · 2021: 12 · 2020: 21 · 2019: 13 · 2018: 11 · 2017: 19 · 2016: 17 · 2015: 32
- FWCI
- 10.96
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- NIH (GM095315, GM107462)
- Topics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Porphyrin Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- translocator protein (TSPO), PK11195, crystal structure, antioxidant defense
- MeSH terms
- Amino Acid Sequence, Bacillus cereus, Bacterial Proteins, Binding Sites, Isoquinolines, Ligands, Molecular Sequence Data, Protein Conformation, Protoporphyrins, Tryptophan, Reactive Oxygen Species, Protein Structure, Secondary, Crystallography, X-Ray, Protein Subunits, Membrane Transport Proteins, Mutant Proteins, Protein Multimerization
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