9YJT
The structure of the periplasmic chaperone Skp from Neisseria meningitidis in space group P21
Summary for 9YJT
| Entry DOI | 10.2210/pdb9yjt/pdb |
| Descriptor | Outer membrane protein H (1 entity in total) |
| Functional Keywords | periplasm, protein folding, chaperone |
| Biological source | Neisseria meningitidis serogroup B |
| Total number of polymer chains | 12 |
| Total formula weight | 205371.74 |
| Authors | |
| Primary citation | Dubey, S.,Stoudenmire, J.,Gheinani, P.T.,Cornelissen, C.N.,Noinaj, N. Structural insight into the role of the periplasmic chaperone Skp in pathogenic Neisseria. Structure, 2026 Cited by PubMed Abstract: Periplasmic chaperones prevent misfolding and aggregation of proteins in the periplasm and those destined for the outer membranes of Gram-negative bacteria. SurA and Skp are two major periplasmic chaperones, with Skp being the most critical in pathogenic Neisseria since its deletion resulted in drastically reduced levels of the porins PorA and PorB and the surface lipoprotein TbpB. Much of what is known about Skp originates from studies in E. coli, where it was observed as a trimer. In our structural studies, however, Skp from N. meningitidis is a hexamer consisting of a dimer of closely packed interdigitated trimers. Constricted and expanded conformations are observed, indicating the arms of the hexamer are flexible and dynamic. We postulate that Skp in Neisseria must utilize a different mechanism than in E. coli to stabilize substrates by expanding and contracting along its long axis to accommodate substrates of differing sizes. PubMed: 42480540DOI: 10.1016/j.str.2026.06.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.14 Å) |
Structure validation
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