24YE
Client peptide-bound structure of a MucD trimer within a 12mer cage
Summary for 24YE
| Entry DOI | 10.2210/pdb24ye/pdb |
| EMDB information | 69907 |
| Descriptor | Probable periplasmic serine endoprotease DegP-like, Peptide from Alginate biosynthesis protein AlgK (2 entities in total) |
| Functional Keywords | protease, cryo-em, hydrolase |
| Biological source | Pseudomonas aeruginosa PAO1 More |
| Total number of polymer chains | 9 |
| Total formula weight | 313143.52 |
| Authors | Jiang, Y.J.,Gao, Y.G. (deposition date: 2026-03-24, release date: 2026-08-26, Last modification date: 2026-09-30) |
| Primary citation | Jiang, Y.,Yan, X.F.,Ero, R.,Wang, C.,Sabapathy, K.,Gao, Y.G. MucD regulates alginate biosynthesis through the proteolytic control of AlgX and AlgK in Pseudomonas aeruginosa. Plos Biol., 24:e3003985-e3003985, 2026 Cited by PubMed Abstract: Pseudomonas aeruginosa is an opportunistic human pathogen capable of infecting a wide range of tissues and organs. Its persistence during chronic infection is strongly associated with biofilm formation, which depends on extracellular polysaccharides such as alginate. The HtrA-like periplasmic serine protease MucD is a key regulator of bacterial virulence, stress response, and alginate production, yet its molecular mechanism has remained largely unclear. Here, we discovered the alginate acetylation and export proteins AlgX and AlgK as MucD substrates, and characterized their degradation by mass spectrometry and bioinformatic analysis. We further determined the cryo-EM structure of MucD bound to an AlgK-derived substrate peptide, offering atomic insights into MucD oligomerization assembly, substrate recognition, and specificity. Together with structure-guided mutagenesis and biochemical assays, our results revealed that MucD proteolytic activity is governed by an equilibrium between a resting 12-mer and an active trimer. Crucially, we demonstrate that MucD represses alginate biosynthesis post-translationally, in addition to its previously implicated role in transcriptional regulation. These findings define a distinct activation mechanism and regulatory function for MucD and provide new insight into bacterial HtrA-like serine proteases. PubMed: 42766672DOI: 10.1371/journal.pbio.3003985 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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