9sln | pdb_00009sln

Zuzalysin bi-pentamer cryo-em

spinqualitylabelsall models 9sln, resolution 2.82Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9sln is a 10 chain structure with sequence from Porphyromonas gingivalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.82Å Ligands: CA, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0AAF0BD41_PORGN Publication Abstract from PubMed Natural pentamer dodecahedra (Ddhs) span six orders of magnitude in diameter. Among proteins, only two catalytic Ddhs have been structurally characterized: lumazine synthase (LS) and the core of pyruvate dehydrogenase (PDH). Zuzalysin (ZUZ) is a approximately 95-kDa metallopeptidase secreted for virulence by Porphyromonas gingivalis. Calcium converts latent flexible monomers into active approximately 0.5-MDa pentamers that further assemble hierarchically into bipentamers, tripentamers, and a approximately 5.6-MDa, approximately 355-A virus-like dodecahedron (Ddh(ZUZ)). Experimental structures (1.8-3.6 A) across these states reveal the molecular basis of activation, association, and catalysis, culminating in Ddh(ZUZ), which is physiologic, exceeds small viral capsids, and has 20 main entry pores and 60 lumen-facing active sites. ZUZ represents the largest catalytic protein assembly resolved at high resolution, exceeding LS, PDH, and major peptidase complexes in size and/or resolution. Structure and Function of a Multi-Megadalton Virus-Like Proteolytic Dodecahedron.,Madej M, Rodriguez-Banqueri A, Mizgalska D, Szmigielski B, Nowakowska Z, Benedyk-Machaczka M, Bzowska M, Mikruta K, Ramirez-Larrota JS, Agunanne C, Julien O, O'Donoghue AJ, Scavenius C, Lopez-Martin M, Marcos E, Koziej L, Glatt S, Guerra P, Eckhard U, Potempa J, Gomis-Ruth FX Angew Chem Int Ed Engl. 2026 Sep 10:e5597279. doi: 10.1002/anie.5597279. PMID:42723362 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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