4KH3
Structure of a bacterial self-associating protein
Summary for 4KH3
| Entry DOI | 10.2210/pdb4kh3/pdb |
| Related | 1DAB 3H09 |
| Descriptor | Antigen 43, MALONATE ION (3 entities in total) |
| Functional Keywords | self-associating protein, uropathogenic escherichia coli, aida-i type autotransporter, ag43, aggregation, biofilm, immune system |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 50883.56 |
| Authors | Heras, B.,Gee, C.L.,Schembri, M.A.,Totsika, M. (deposition date: 2013-04-30, release date: 2014-01-15, Last modification date: 2024-03-20) |
| Primary citation | Heras, B.,Totsika, M.,Peters, K.M.,Paxman, J.J.,Gee, C.L.,Jarrott, R.J.,Perugini, M.A.,Whitten, A.E.,Schembri, M.A. The antigen 43 structure reveals a molecular Velcro-like mechanism of autotransporter-mediated bacterial clumping. Proc.Natl.Acad.Sci.USA, 111:457-462, 2014 Cited by PubMed Abstract: Aggregation and biofilm formation are critical mechanisms for bacterial resistance to host immune factors and antibiotics. Autotransporter (AT) proteins, which represent the largest group of outer-membrane and secreted proteins in Gram-negative bacteria, contribute significantly to these phenotypes. Despite their abundance and role in bacterial pathogenesis, most AT proteins have not been structurally characterized, and there is a paucity of detailed information with regard to their mode of action. Here we report the structure-function relationships of Antigen 43 (Ag43a), a prototypic self-associating AT protein from uropathogenic Escherichia coli. The functional domain of Ag43a displays a twisted L-shaped β-helical structure firmly stabilized by a 3D hydrogen-bonded scaffold. Notably, the distinctive Ag43a L shape facilitates self-association and cell aggregation. Combining all our data, we define a molecular "Velcro-like" mechanism of AT-mediated bacterial clumping, which can be tailored to fit different bacterial lifestyles such as the formation of biofilms. PubMed: 24335802DOI: 10.1073/pnas.1311592111 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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