3BB7
Structure of Prevotella intermedia prointerpain A fragment 39-359 (mutant C154A)
Summary for 3BB7
| Entry DOI | 10.2210/pdb3bb7/pdb |
| Related | 3BBA |
| Descriptor | interpain A (2 entities in total) |
| Functional Keywords | cysteine protease, zymogen activation, bacterial odontopathogen, hydrolase |
| Biological source | Prevotella intermedia |
| Total number of polymer chains | 1 |
| Total formula weight | 35062.93 |
| Authors | Mallorqui-Fernandez, N.,Manandhar, S.P.,Mallorqui-Fernandez, G.,Uson, I.,Wawrzonek, K.,Kantyka, T.,Sola, M.,Thogersen, I.B.,Enghild, J.J.,Potempa, J.,Gomis-Ruth, F.X. (deposition date: 2007-11-09, release date: 2007-11-20, Last modification date: 2023-11-01) |
| Primary citation | Mallorqui-Fernandez, N.,Manandhar, S.P.,Mallorqui-Fernandez, G.,Uson, I.,Wawrzonek, K.,Kantyka, T.,Sola, M.,Thogersen, I.B.,Enghild, J.J.,Potempa, J.,Gomis-Ruth, F.X. A New Autocatalytic Activation Mechanism for Cysteine Proteases Revealed by Prevotella intermedia Interpain A J.Biol.Chem., 283:2871-2882, 2008 Cited by PubMed Abstract: Prevotella intermedia is a major periodontopathogen contributing to human gingivitis and periodontitis. Such pathogens release proteases as virulence factors that cause deterrence of host defenses and tissue destruction. A new cysteine protease from the cysteine-histidine-dyad class, interpain A, was studied in its zymogenic and self-processed mature forms. The latter consists of a bivalved moiety made up by two subdomains. In the structure of a catalytic cysteine-to-alanine zymogen variant, the right subdomain interacts with an unusual prodomain, thus contributing to latency. Unlike the catalytic cysteine residue, already in its competent conformation in the zymogen, the catalytic histidine is swung out from its active conformation and trapped in a cage shaped by a backing helix, a zymogenic hairpin, and a latency flap in the zymogen. Dramatic rearrangement of up to 20A of these elements triggered by a tryptophan switch occurs during activation and accounts for a new activation mechanism for proteolytic enzymes. These findings can be extrapolated to related potentially pathogenic cysteine proteases such as Streprococcus pyogenes SpeB and Porphyromonas gingivalis periodontain. PubMed: 17993455DOI: 10.1074/jbc.M708481200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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