结核分枝杆菌精氨琥珀酸裂解酶（Rv1659）的克隆、表达、纯化、结晶及初步X射线研究
Cloning, expression, purification, crystallization and preliminary X-ray studies of argininosuccinate lyase (Rv1659) from Mycobacterium tuberculosis.
作者信息
Paul A, Mishra A, Surolia A, Vijayan M
机构信息
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1422-4. doi: 10.1107/S1744309113031138. Epub 2013 Nov 29.
Abstract
The last enzyme in the arginine-biosynthesis pathway, argininosuccinate lyase, from Mycobacterium tuberculosis has been cloned, expressed, purified and crystallized, and preliminary X-ray studies have been carried out on the crystals. The His-tagged tetrameric enzyme with a subunit molecular weight of 50.9 kDa crystallized with two tetramers in the asymmetric unit of the orthorhombic unit cell, space group P2(1)2(1)2(1). Molecular-replacement calculations and self-rotation calculations confirmed the space group and the tetrameric nature of the molecule.
摘要
结核分枝杆菌精氨酸生物合成途径中的最后一种酶——精氨琥珀酸裂解酶，已被克隆、表达、纯化并结晶，且已对晶体进行了初步的X射线研究。该带有组氨酸标签的四聚体酶，亚基分子量为50.9 kDa，在正交晶胞的不对称单元中与两个四聚体一起结晶，空间群为P2(1)2(1)2(1)。分子置换计算和自旋转计算证实了该分子的空间群和四聚体性质。
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