2M0Z
cis form of a photoswitchable PDZ domain crosslinked with an azobenzene derivative
Summary for 2M0Z
| Entry DOI | 10.2210/pdb2m0z/pdb |
| Related | 2M10 |
| NMR Information | BMRB: 18833 |
| Descriptor | Tyrosine-protein phosphatase non-receptor type 13, 3,3'-(E)-diazene-1,2-diylbis{6-[(chloroacetyl)amino]benzenesulfonic acid} (2 entities in total) |
| Functional Keywords | photoswitch, hydrolase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm, cytoskeleton (By similarity): Q12923 |
| Total number of polymer chains | 1 |
| Total formula weight | 10592.74 |
| Authors | Walser, R.,Zerbe, O.,Hamm, P. (deposition date: 2012-11-09, release date: 2013-07-03, Last modification date: 2025-03-26) |
| Primary citation | Buchli, B.,Waldauer, S.A.,Walser, R.,Donten, M.L.,Pfister, R.,Blochliger, N.,Steiner, S.,Caflisch, A.,Zerbe, O.,Hamm, P. Kinetic response of a photoperturbed allosteric protein. Proc.Natl.Acad.Sci.USA, 110:11725-11730, 2013 Cited by PubMed Abstract: By covalently linking an azobenzene photoswitch across the binding groove of a PDZ domain, a conformational transition, similar to the one occurring upon ligand binding to the unmodified domain, can be initiated on a picosecond timescale by a laser pulse. The protein structures have been characterized in the two photoswitch states through NMR spectroscopy and the transition between them through ultrafast IR spectroscopy and molecular dynamics simulations. The binding groove opens on a 100-ns timescale in a highly nonexponential manner, and the molecular dynamics simulations suggest that the process is governed by the rearrangement of the water network on the protein surface. We propose this rearrangement of the water network to be another possible mechanism of allostery. PubMed: 23818626DOI: 10.1073/pnas.1306323110 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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