5U8E

Crystal Structure of substrate-free arginine kinase from spider Polybetes pythagoricus

5U8E の概要

• エントリーDOI: 10.2210/pdb5u8e/pdb
• 関連するPDBエントリー: 5U92
• 分子名称: arginine kinase, SODIUM ION (3 entities in total)
• 機能のキーワード: phosphagen metabolism, arginine kinase, spider, open conformation, free-ligand, transferase
• 由来する生物種: Polybetes pythagoricus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43314.03

構造登録者

Lopez-Zavala, A.A.,Garcia, C.F.,Hernadez-Paredes, J.,Sotelo-Mundo, R.R. (登録日: 2016-12-14, 公開日: 2017-08-30, 最終更新日: 2024-10-09)

主引用文献

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

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: 28924503
DOI: 10.7717/peerj.3787

実験手法

X-RAY DIFFRACTION (2.18 Å)