2X7Z
Crystal Structure of the SAP97 PDZ2 I342W C378A mutant protein domain
Summary for 2X7Z
| Entry DOI | 10.2210/pdb2x7z/pdb |
| Related | 1PDR |
| Descriptor | DISKS LARGE HOMOLOG 1, AMMONIUM ION, IMIDAZOLE, ... (4 entities in total) |
| Functional Keywords | sh3 domain, phosphoprotein, synaptic protein, host-virus interaction, structural protein |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 1 |
| Total formula weight | 10571.15 |
| Authors | Haq, S.R.,Jurgens, M.C.,Chi, C.N.,Elfstrom, L.,Koh, C.S.,Selmer, M.,Gianni, S.,Jemth, P. (deposition date: 2010-03-04, release date: 2010-03-31, Last modification date: 2023-12-20) |
| Primary citation | Haq, S.R.,Jurgens, M.C.,Chi, C.N.,Elfstrom, L.,Koh, C.S.,Selmer, M.,Gianni, S.,Jemth, P. The Plastic Energy Landscape of Protein Folding: A Triangular Folding Mechanism with an Equilibrium Intermediate for a Small Protein Domain. J.Biol.Chem., 285:18051-, 2010 Cited by PubMed Abstract: Protein domains usually fold without or with only transiently populated intermediates, possibly to avoid misfolding, which could result in amyloidogenic disease. Whether observed intermediates are productive and obligatory species on the folding reaction pathway or dispensable by-products is a matter of debate. Here, we solved the crystal structure of a small protein domain, SAP97 PDZ2 I342W C378A, and determined its folding pathway. The presence of a folding intermediate was demonstrated both by single and double-mixing kinetic experiments using urea-induced (un)folding as well as ligand-induced folding. This protein domain was found to fold via a triangular scheme, where the folding intermediate could be either on- or off-pathway, depending on the experimental conditions. Furthermore, we found that the intermediate was present at equilibrium, which is rarely seen in folding reactions of small protein domains. The folding mechanism observed here illustrates the roughness and plasticity of the protein folding energy landscape, where several routes may be employed to reach the native state. The results also reconcile the folding mechanisms of topological variants within the PDZ domain family. PubMed: 20356847DOI: 10.1074/JBC.M110.110833 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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