4ZGH
Structure of Sugar Binding Protein Pneumolysin
Summary for 4ZGH
| Entry DOI | 10.2210/pdb4zgh/pdb |
| Descriptor | Pneumolysin, 1,2-ETHANEDIOL, DI(HYDROXYETHYL)ETHER, ... (5 entities in total) |
| Functional Keywords | beta-cft, toxin, sugar binding protein |
| Biological source | Streptococcus pneumoniae |
| Total number of polymer chains | 1 |
| Total formula weight | 54692.40 |
| Authors | Parker, M.W.,Feil, S.C.,Morton, C. (deposition date: 2015-04-23, release date: 2016-03-09, Last modification date: 2023-09-27) |
| Primary citation | Lawrence, S.L.,Feil, S.C.,Morton, C.J.,Farrand, A.J.,Mulhern, T.D.,Gorman, M.A.,Wade, K.R.,Tweten, R.K.,Parker, M.W. Crystal structure of Streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation. Sci Rep, 5:14352-14352, 2015 Cited by PubMed Abstract: Pore-forming proteins are weapons often used by bacterial pathogens to breach the membrane barrier of target cells. Despite their critical role in infection important structural aspects of the mechanism of how these proteins assemble into pores remain unknown. Streptococcus pneumoniae is the world's leading cause of pneumonia, meningitis, bacteremia and otitis media. Pneumolysin (PLY) is a major virulence factor of S. pneumoniae and a target for both small molecule drug development and vaccines. PLY is a member of the cholesterol-dependent cytolysins (CDCs), a family of pore-forming toxins that form gigantic pores in cell membranes. Here we present the structure of PLY determined by X-ray crystallography and, in solution, by small-angle X-ray scattering. The crystal structure reveals PLY assembles as a linear oligomer that provides key structural insights into the poorly understood early monomer-monomer interactions of CDCs at the membrane surface. PubMed: 26403197DOI: 10.1038/srep14352 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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