5loy | pdb_00005loy

Helical Assembly of a Designed Anbu Protein

spinqualitylabelsall models 5loy, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5loy is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Proteasomes are self-compartmentalizing proteases that function at the core of the cellular protein degradation machinery in eukaryotes, archaea, and some bacteria. Although their evolutionary history is under debate, it is thought to be linked to that of the bacterial protease HslV and the hypothetical bacterial protease Anbu (ancestral beta subunit). Here, together with an extensive bioinformatic analysis, we present the first biophysical characterization of Anbu. Anbu forms a dodecameric complex with a unique architecture that was only accessible through the combination of X-ray crystallography and small-angle X-ray scattering. While forming continuous helices in crystals and electron microscopy preparations, refinement of sections from the crystal structure against the scattering data revealed a helical open-ring structure in solution, contrasting the ring-shaped structures of proteasome and HslV. Based on this primordial architecture and exhaustive sequence comparisons, we propose that Anbu represents an ancestral precursor at the origin of self-compartmentalization. The Architecture of the Anbu Complex Reflects an Evolutionary Intermediate at the Origin of the Proteasome System.,Fuchs ACD, Alva V, Maldoner L, Albrecht R, Hartmann MD, Martin J Structure. 2017 Jun 6;25(6):834-845.e5. doi: 10.1016/j.str.2017.04.005. Epub 2017, May 4. PMID:28479063 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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