3T8O
Rhodopsin kinase (GRK1) L166K mutant at 2.5A resolution
Summary for 3T8O
| Entry DOI | 10.2210/pdb3t8o/pdb |
| Related | 3c4w 3c4x |
| Descriptor | Rhodopsin kinase, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | kinase domain, rgs homology (rh) domain, g-protein receptor kinase (gpcr), transferase |
| Biological source | Bos taurus (bovine,cow,domestic cattle,domestic cow) |
| Cellular location | Membrane ; Lipid- anchor : P28327 |
| Total number of polymer chains | 1 |
| Total formula weight | 62104.99 |
| Authors | Tesmer, J.J.G.,Singh, P.,Nance, M.R. (deposition date: 2011-08-01, release date: 2012-06-06, Last modification date: 2024-02-28) |
| Primary citation | Tesmer, J.J.,Nance, M.R.,Singh, P.,Lee, H. Structure of a monomeric variant of rhodopsin kinase at 2.5 A resolution. Acta Crystallogr.,Sect.F, 68:622-625, 2012 Cited by PubMed Abstract: G protein-coupled receptor kinase 1 (GRK1 or rhodopsin kinase) phosphorylates activated rhodopsin and initiates a cascade of events that results in the termination of phototransduction by the receptor. Although GRK1 seems to be a monomer in solution, seven prior crystal structures of GRK1 revealed a similar domain-swapped dimer interface involving the C-terminus of the enzyme. The influence of this interface on the overall conformation of GRK1 is not known. To address this question, the crystalline dimer interface was disrupted with a L166K mutation and the structure of GRK1-L166K was determined in complex with Mg(2+) · ATP to 2.5 Å resolution. GRK1-L166K crystallized in a novel space group as a monomer and exhibited little overall conformational difference from prior structures of GRK1, although the C-terminal domain-swapped region had reorganized owing to loss of the dimer interface. PubMed: 22684056DOI: 10.1107/S1744309112017435 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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