9SM8
Zuzalysin zymogen pentamer E439A
Summary for 9SM8
| Entry DOI | 10.2210/pdb9sm8/pdb |
| Related | 9SLB 9SLL 9SLN 9SM4 |
| EMDB information | 55026 55028 55505 55508 |
| Descriptor | Zinc-dependent metalloprotease, CALCIUM ION, ZINC ION (3 entities in total) |
| Functional Keywords | metallopeptidase, pentamer, zymogen, prophyromonas gingivalis, hydrolase |
| Biological source | Porphyromonas gingivalis |
| Total number of polymer chains | 5 |
| Total formula weight | 486043.96 |
| Authors | Rodriguez-Banqueri, A.,Madej, M.,Eckhard, U.,Potempa, J.,Gomis Ruth, F.X. (deposition date: 2025-09-05, release date: 2026-09-16, Last modification date: 2026-09-23) |
| Primary citation | Madej, M.,Rodriguez-Banqueri, A.,Mizgalska, D.,Szmigielski, B.,Nowakowska, Z.,Benedyk-Machaczka, M.,Bzowska, M.,Mikruta, K.,Ramirez-Larrota, J.S.,Agunanne, C.,Julien, O.,O'Donoghue, A.J.,Scavenius, C.,Lopez-Martin, M.,Marcos, E.,Koziej, L.,Glatt, S.,Guerra, P.,Eckhard, U.,Potempa, J.,Gomis-Ruth, F.X. Structure and Function of a Multi-Megadalton Virus-Like Proteolytic Dodecahedron. Angew.Chem.Int.Ed.Engl., :e5597279-e5597279, 2026 Cited by PubMed Abstract: 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 ≈95-kDa metallopeptidase secreted for virulence by Porphyromonas gingivalis. Calcium converts latent flexible monomers into active ≈0.5-MDa pentamers that further assemble hierarchically into bipentamers, tripentamers, and a ≈5.6-MDa, ≈355-Å virus-like dodecahedron (Ddh). Experimental structures (1.8-3.6 Å) across these states reveal the molecular basis of activation, association, and catalysis, culminating in Ddh, 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. PubMed: 42723362DOI: 10.1002/anie.5597279 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.59 Å) |
Structure validation
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