4AM1

Crystal structure of the marine crustacean decapod shrimp (Litopenaeus vannamei) arginine kinase in the absence of substrate or ligands.

4AM1 の概要

• エントリーDOI: 10.2210/pdb4am1/pdb
• 分子名称: ARGININE KINASE (2 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: LITOPENAEUS VANNAMEI (WHITELEG SHRIMP)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40028.60

構造登録者

Lopez-Zavala, A.A.,Sotelo-Mundo, R.R.,Garcia-Orozco, K.D.,Isac-Martinez, F.,Brieba, L.G.,Rudino-Pinera, E. (登録日: 2012-03-07, 公開日: 2012-07-11, 最終更新日: 2024-05-01)

主引用文献

Lopez-Zavala, A.A.,Sotelo-Mundo, R.R.,Garcia-Orozco, K.D.,Isac-Martinez, F.,Brieba, L.G.,Rudino-Pinera, E.
Crystallization and X-Ray Diffraction Studies of Arginine Kinase from the White Pacific Shrimp Litopenaeus Vannamei.
Acta Crystallogr.,Sect.F, 68:783-, 2012

PubMed Abstract: Crystals of an unligated monomeric arginine kinase from the Pacific whiteleg shrimp Litopenaeus vannamei (LvAK) were successfully obtained using the microbatch method. Crystallization conditions and preliminary X-ray diffraction analysis to 1.25 Å resolution are reported. Data were collected at 100 K on NSLS beamline X6A. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 56.5, b = 70.2, c = 81.7 Å. One monomer per asymmetric unit was found, with a Matthews coefficient (V(M)) of 2.05 Å(3) Da(-1) and 40% solvent content. Initial phases were determined by molecular replacement using a homology model of LvAK as the search model. Refinement was performed with PHENIX, with final R(work) and R(free) values of 0.15 and 0.19, respectively. Biological analysis of the structure is currently in progress.

PubMed: 22750864
DOI: 10.1107/S1744309112020180

実験手法

X-RAY DIFFRACTION (1.25 Å)