5nyw

Anbu (ancestral beta-subunit) from Yersinia bercovieri

spinqualitylabelsall models 5nyw, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5nyw is a 28 chain structure with sequence from Yersinia bercovieri. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AZI, CL, EDO, PEG, SO4, UNX Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A2G4U6U6_YERBE Publication Abstract from PubMed Anbu (ancestral beta-subunit) is homologous to HslV and 20S proteasomes. Based on its phylogenetic distribution and sequence clustering, Anbu has been proposed as the "ancestral" form of proteasomes. Here, we report biochemical data, small-angle X-ray scattering (SAXS) results, negative stain electron microscopy (EM) micrographs, and a crystal structure of the Anbu particle from Yersinia bercovieri (YbAnbu). All data are consistent with YbAnbu forming defined 12-14 subunit multimers that differ in shape from both HslV and 20S proteasomes. The crystal structure reveals that YbAnbu subunits form tight dimers, held together in part by the Anbu specific C-terminal helices. These dimers ("protomers") further assemble into a low rise left-handed staircase. The lock-washer shape of YbAnbu is consistent with the presence of defined multimers, X-ray diffraction data in solution and negative stain electron microscopy images. The presented structure suggests a possible evolutionary pathway from helical filaments to highly symmetric or pseudosymmetric multimer structures. YbAnbu subunits have the Ntn-hydrolase fold, a putative S1 pocket and conserved candidate catalytic residues Thr1, Asp17 and Lys32(33). Nevertheless, we did not detect any YbAnbu peptidase or amidase activity. However, we could document orthophosphate production from ATP catalyzed by the ATP-grasp protein encoded in the Yersinia bercovieri Anbu operon. The Y. bercovieri Anbu crystal structure sheds light on the evolution of highly (pseudo)symmetric multimers.,Piasecka A, Czapinska H, Vielberg MT, Szczepanowski R, Kiefersauer R, Reed S, Groll M, Bochtler M J Mol Biol. 2017 Dec 16. pii: S0022-2836(17)30590-9. doi:, 10.1016/j.jmb.2017.11.016. PMID:29258816 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Proteasome 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA