4GW0
Crystal structure of arginine kinase in complex with imino-L-ornithine, MgADP, and nitrate.
Summary for 4GW0
| Entry DOI | 10.2210/pdb4gw0/pdb |
| Related | 1M15 3M10 4GVY 4GVZ 4GW2 |
| Descriptor | Arginine kinase, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | arginine kinase, phosphagen kinase, transferase, transition state analog, kinase |
| Biological source | Limulus polyphemus (Atlantic horseshoe crab) |
| Cellular location | Cytoplasm: P51541 |
| Total number of polymer chains | 1 |
| Total formula weight | 40936.48 |
| Authors | Clark, S.A.,Davulcu, O.,Chapman, M.S. (deposition date: 2012-08-31, release date: 2012-10-03, Last modification date: 2023-09-13) |
| Primary citation | Clark, S.A.,Davulcu, O.,Chapman, M.S. Crystal structures of arginine kinase in complex with ADP, nitrate, and various phosphagen analogs. Biochem.Biophys.Res.Commun., 427:212-217, 2012 Cited by PubMed Abstract: Arginine kinase catalyzes the reversible transfer of a phosphoryl group between ATP and l-arginine and is a monomeric homolog of the human enzyme creatine kinase. Arginine and creatine kinases belongs to the phosphagen kinase family of enzymes, which consists of eight known members, each of which is specific for its own phosphagen. Here, the source of phosphagen specificity in arginine kinase is investigated through the use of phosphagen analogs. Crystal structures have been determined for Limulus polyphemus arginine kinase with one of four arginine analogs bound in a transition state analog complex: l-ornithine, l-citrulline, imino-l-ornithine, and d-arginine. In all complexes, the enzyme achieves a closed conformation very similar to that of the cognate transition state analog complex, but differences are observed in the configurations of bound ligands. Arginine kinase exhibits no detectable activity towards ornithine, citrulline, or imino-l-ornithine, and only trace activity towards d-arginine. The crystal structures presented here demonstrate that phosphagen specificity is derived neither from a lock-and-key mechanism nor a modulation of induced-fit conformational changes, but potentially from subtle distortions in bound substrate configurations. PubMed: 22995310DOI: 10.1016/j.bbrc.2012.09.053 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.448 Å) |
Structure validation
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