5U8E
Crystal Structure of substrate-free arginine kinase from spider Polybetes pythagoricus
Summary for 5U8E
| Entry DOI | 10.2210/pdb5u8e/pdb |
| Related | 5U92 |
| Descriptor | arginine kinase, SODIUM ION (3 entities in total) |
| Functional Keywords | phosphagen metabolism, arginine kinase, spider, open conformation, free-ligand, transferase |
| Biological source | Polybetes pythagoricus |
| Total number of polymer chains | 1 |
| Total formula weight | 43314.03 |
| Authors | Lopez-Zavala, A.A.,Garcia, C.F.,Hernadez-Paredes, J.,Sotelo-Mundo, R.R. (deposition date: 2016-12-14, release date: 2017-08-30, Last modification date: 2024-10-09) |
| Primary citation | Laino, A.,Lopez-Zavala, A.A.,Garcia-Orozco, K.D.,Carrasco-Miranda, J.S.,Santana, M.,Stojanoff, V.,Sotelo-Mundo, R.R.,Garcia, C.F. Biochemical and structural characterization of a novel arginine kinase from the spider Polybetes pythagoricus. PeerJ, 5:e3787-e3787, 2017 Cited by PubMed Abstract: Energy buffering systems are key for homeostasis during variations in energy supply. Spiders are the most important predators for insects and therefore key in terrestrial ecosystems. From biomedical interest, spiders are important for their venoms and as a source of potent allergens, such as arginine kinase (AK, EC 2.7.3.3). AK is an enzyme crucial for energy metabolism, keeping the pool of phosphagens in invertebrates, and also an allergen for humans. In this work, we studied AK from the Argentininan spider (AK), from its complementary DNA to the crystal structure. The AK cDNA from muscle was cloned, and it is comprised of 1068 nucleotides that encode a 384-amino acids protein, similar to other invertebrate AKs. The apparent Michaelis-Menten kinetic constant ( ) was 1.7 mM with a of 75 s. Two crystal structures are presented, the apoAK and AK bound to arginine, both in the conformation with the active site lid (residues 310-320) completely disordered. The guanidino group binding site in the apo structure appears to be organized to accept the arginine substrate. Finally, these results contribute to knowledge of mechanistic details of the function of arginine kinase. PubMed: 28924503DOI: 10.7717/peerj.3787 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.18 Å) |
Structure validation
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