Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein
Open accessAbstract
Human p32 (also known as SF2-associated p32, p32/TAP, and gC1qR) is a conserved eukaryotic protein that localizes predominantly in the mitochondrial matrix. It is thought to be involved in mitochondrial oxidative phosphorylation and in nucleus–mitochondrion interactions. We report the crystal structure of p32 determined at 2.25 Å resolution. The structure reveals that p32 adopts a novel fold with seven consecutive antiparallel β-strands flanked by one N-terminal and two C-terminal α-helices. Three monomers form a doughnut-shaped quaternary structure with an unusually asymmetric charge distribution on the surface. The implications of the structure on previously proposed functions of p32 are discussed and new specific functional properties are suggested.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
p32 predominantly localizes in mitochondria and is a recognized RNA-binding protein within the mitochondrial context.
“p32, a well-conserved eukaryotic protein that predominantly localizes in mitochondria (Barna et al, 2019; Gotoh et al, 2018), serves as a recognized RNA-binding protein within the mitochondrial context.”
From The mitochondrial long non-coding RNA lncMtloop regulates mitochondrial transcription and suppresses Alzheimer’s disease (2024) · cites this paper as Jiang et al, 1999
The paper’s introductory discussion says p32 localizes predominantly in the mitochondrial matrix, and the Discussion reiterates that it is mainly mitochondrial under normal conditions. The passages found do not identify p32 as an RNA-binding protein in mitochondria; they describe its association with a pre-mRNA splicing factor but note that no splicing function was established. (LLM, conf=0.85)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Fridell, R. A., Harding, L. S., Bogerd, H. P., & Cullen, B. R. (1995) · Virology · doi:10.1006/viro.1995.1266 · Cited by 129 · see citing works
McCormack, J. G., & Denton, R. M. (1993) · Biochemical Society Transactions · doi:10.1042/bst0210793 · Cited by 94 · see citing works
Flagged first, then by citations
Research works printed but not linked: 4
- [2]Desai, K., Loewenstein, P. M. & Green, M. (1991) Proc. Natl. Acad. Sci. USA 88, 8875-8879.
- [8]Bruni, R. & Roizman, B. (1996) Proc. Natl. Acad. Sci. USA 93, 10423-10427.
- [20]Otwinowski, Z. (1993) Data Collection and Processing Proceedings of the CCP4 Study Weekend, eds. Sawyer, L., Issacs, N. & Bailey, S. (Science and Engineering Research Council, Daresbury Laboratory, Warrington, U.K.) pp. 56-62.
- [36]McCormack, J. G. & Denton, R. M. (1993) Biochem. Soc. Trans. 21 (Pt 3), 793-799.
Cited by
Sorted by citations
Mitochondria in innate immune responses
West, A. P., Shadel, G. S., & Ghosh, S. (2011) · Nature Reviews Immunology · doi:10.1038/nri2975 · Cited by 1,376 · see citing works
Hyaluronan-binding Proteins: Tying Up the Giant
Day, A. J., & Prestwich, G. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.r100036200 · Cited by 567 · see citing works
Molecular bases of progeroid syndromes
Navarro, C. L., Cau, P., & Lévy, N. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl214 · Cited by 189 · see citing works
Towards a structural understanding of Friedreich’s ataxia: the solution structure of frataxin
Musco, G., Stier, G., Kolmerer, B., Adinolfi, S., Martin, S., Frenkiel, T., Gibson, T., & Pastore, A. (2000) · Structure · doi:10.1016/s0969-2126(00)00158-1 · Cited by 166 · see citing works
Yagi, M., Uchiumi, T., Takazaki, S., Okuno, B., Nomura, M., Yoshida, S.-I., Kanki, T., & Kang, D. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks774 · Cited by 169 · see citing works
Gao, Y., Colletti, K., & Pari, G. S. (2008) · Journal of Virology · doi:10.1128/jvi.01559-07 · Cited by 58 · see citing works
Xiong, W., Xu, K., Sun, J. K.-L., Liu, S., Zhao, B., Shi, J., Herrup, K., Chow, H.-M., Lu, L., & Li, J. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00270-7 · Cited by 17 · see citing works
“Its functions extend to in fl uencing the regulation of OXPHOS, orchestrating communication between the nucleus and mitochondria, and participating in other mitochondrial activities (Jiang et al, 1999; Leucci et al, 2016; Yagi et al, 2012).”
- Authors
- Jiang, J., Zhang, Y., Krainer, A. R., & Xu, R.-M.
- Affiliations
- Cold Spring Harbor Laboratory (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1999-03-30
- Volume
- 96
- Issue
- 7
- Pages
- 3572-3577
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC22335
- OpenAlex
- W1967493968
- Cited by
- 253
- References
- 2
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 10 · 2023: 9 · 2022: 14 · 2021: 15 · 2020: 10 · 2019: 9 · 2018: 5 · 2017: 11 · 2016: 6 · 2015: 8 · 2014: 5 · 2013: 9 · 2012: 11
- FWCI
- 9.42
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Cold Spring Harbor Laboratory Institutional Repository (Cold Spring Harbor Laboratory) (acceptedVersion)
- Funders
- W. M. Keck Foundation
- National Institutes of Health (CA13106)
- National Cancer Institute (CA13106, P01CA013106)
- National Institute of General Medical Sciences (GM55874, R01GM055874)
- Brookhaven National Laboratory
- Topics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- p32, gC1qR, mitochondrial matrix proteins, novel protein fold, antiparallel beta-strands, oxidative phosphorylation, protein crystal structure
- MeSH terms
- Amino Acid Sequence, Animals, Caenorhabditis, Carrier Proteins, Computer Graphics, Humans, Membrane Glycoproteins, Mitochondria, Models, Molecular, Molecular Sequence Data, Protein Conformation, Receptors, Complement, Recombinant Proteins, Saccharomyces cerevisiae, Sequence Alignment, Sequence Homology, Amino Acid, Protein Structure, Secondary, Protein Folding, Crystallography, X-Ray, Hyaluronan Receptors, Mitochondrial Proteins, Macromolecular Substances, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
