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Asymmetric horseshoe-like assembly of peroxisomal Yeast Oxalyl-CoA synthetase
Open accessPreprint — published as 10.1515/hsz-2022-0273
Abstract
Oxalyl-CoA synthetase from Saccharomyces cerevisiae is one of the most abundant peroxisomal protein in yeast and hence has become a model to study peroxisomal translocation. It contains a C-terminal Peroxisome Targeting Signal 1, which however is partly dispensable, suggesting additional receptor bindings sites. To unravel any additional features that may contribute to its capacity to be recognized as peroxisomal target, we determined its assembly and overall architecture by an integrated structural biology approach, including X-ray crystallography, single particle cryo-electron microscopy and small angle X-ray scattering. Surprisingly, it assembles into mixture of concentration-dependent dimers, tetramers and hexamers by dimer self-association. Hexameric particles form an unprecedented asymmetric horseshoe-like arrangement, which considerably differs from symmetric hexameric assembly found in many other protein structures. A single mutation within the self-association interface is sufficient to abolish any higher-level oligomerization, resulting in homogenous dimeric assembly. The small C-terminal domain of yeast Oxalyl-CoA synthetase is connected by a partly flexible hinge with the large N-terminal domain, which provides the sole basis for oligomeric assembly. Our data provide a basis to mechanistically study peroxisomal translocation of this target.
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Metadata
- Authors
- Bürgi, J., Lill, P., Giannopoulou, E.-A., Jeffries, C. M., Chojnowski, G., Raunser, S., Gatsogiannis, C., & Wilmanns, M.
- Affiliations
- European Molecular Biology Laboratory (DE)
- University of Münster (DE)
- Max Planck Institute of Molecular Physiology (DE)
- Universität Hamburg (DE)
- Corresponding author
- Gatsogiannis, Christos
- Wilmanns, Matthias
- ORCID
- Venue
- bioRxiv (Cold Spring Harbor Laboratory)
- Publisher
- openRxiv
- Published
- 2022-08-30
- OpenAlex
- W4294308155
- Cited by
- 1
- References
- 1
- Citations by year
- 2025: 1
- Type
- posted content
- Language
- en
- Open access
- green
- doi.org
- Locations
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- Desy Publications Database (Deutsches Elektronen-Synchrotron DESY) (submittedVersion, other-oa)
- Funders
- European Commission (316723, 664726)
- Deutsche Forschungsgemeinschaft (FOR 1905 (PerTrans consortium) GA 2519/1-2, FOR1905, GA 2519/1-2)
- European Synchrotron Radiation Facility (ID30A-1)
- Deutsches Elektronen-Synchrotron
- H2020 Marie Skłodowska-Curie Actions (316723, 664726)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Keywords
- protein oligomerization, hinge flexibility, Saccharomyces cerevisiae, peroxisomal proteins
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