8ATD
Wild type hexamer oxalyl-CoA synthetase (OCS)
Summary for 8ATD
| Entry DOI | 10.2210/pdb8atd/pdb |
| EMDB information | 15646 |
| Descriptor | Oxalate--CoA ligase (1 entity in total) |
| Functional Keywords | peroxisome, oxalyl-coa ligase, oligomer, yeast, ligase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 6 |
| Total formula weight | 288814.99 |
| Authors | Lill, P.,Burgi, J.,Raunser, S.,Wilmanns, M.,Gatsogiannis, C. (deposition date: 2022-08-23, release date: 2023-02-08, Last modification date: 2024-07-24) |
| Primary citation | Burgi, J.,Lill, P.,Giannopoulou, E.A.,Jeffries, C.M.,Chojnowski, G.,Raunser, S.,Gatsogiannis, C.,Wilmanns, M. Asymmetric horseshoe-like assembly of peroxisomal yeast oxalyl-CoA synthetase. Biol.Chem., 404:195-207, 2023 Cited by PubMed Abstract: Oxalyl-CoA synthetase from is one of the most abundant peroxisomal proteins 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 a 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. PubMed: 36694962DOI: 10.1515/hsz-2022-0273 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
Download full validation report
