1OYU
Long-Distance conformational changes in a protein engineered by modulated sequence duplication
Summary for 1OYU
Entry DOI | 10.2210/pdb1oyu/pdb |
Related | 261L 262L |
Descriptor | Lysozyme (2 entities in total) |
Functional Keywords | sequence duplication, design of structural switches, tandem repeat, protein design, hydrolase |
Biological source | Enterobacteria phage T4 |
Total number of polymer chains | 2 |
Total formula weight | 39026.72 |
Authors | Sagermann, M.,Gay, L.,Matthews, B.W. (deposition date: 2003-04-07, release date: 2003-07-08, Last modification date: 2023-08-16) |
Primary citation | Sagermann, M.,Gay, L.,Matthews, B.W. Long-distance conformational changes in a protein engineered by modulated sequence duplication Proc.Natl.Acad.Sci.USA, 100:9191-9195, 2003 Cited by PubMed Abstract: There are few, if any, known instances in which a biological signal is transmitted via a large conformational change through the body of a protein. We describe here a mutant of T4 lysozyme that was engineered to permit structural change at a distance. The design uses a tandem sequence repeat that makes it possible to transmit large-scale structural changes from one end of an alpha-helix to the other over a distance of 17-25 A. The method should be of general applicability and may make it possible to introduce a mutation at one site in a protein that will induce large-scale changes in the structure at a spatially remote site. PubMed: 12869697DOI: 10.1073/pnas.1633549100 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
Download full validation report