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9SMJ

Zuzalysin zymogen dodecahedral complex E439A

This is a non-PDB format compatible entry.
Summary for 9SMJ
Entry DOI10.2210/pdb9smj/pdb
Related9SLB 9SLL 9SLN 9SM4 9SM8
EMDB information55005 55008 55026 55028 55035
DescriptorZinc-dependent metalloprotease, CALCIUM ION, ZINC ION (3 entities in total)
Functional Keywordsmetallopeptidase, dodecahedral complex, zymogen, prophyromonas gingivalis, hydrolase
Biological sourcePorphyromonas gingivalis
Total number of polymer chains60
Total formula weight5834932.20
Authors
Rodriguez-Banqueri, A.,Madej, M.,Eckhard, U.,Potempa, J. (deposition date: 2025-09-08, release date: 2026-09-23)
Primary citationMadej, 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: 42723362
DOI: 10.1002/anie.5597279
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.64 Å)
Structure validation

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