Crystallization and preliminary X-ray diffraction analysis of the S-adenosylhomocysteine hydrolase (SAHH) from Thermotoga maritima

被引：1

作者：

He, Miao ^{[1
]}

Zheng, Yingying ^{[2
]}

Huang, Chun-Hsiang ^{[2
]}

Qian, Guojun ^{[3
]}

Xiao, Xiansha ^{[2
]}

Ko, Tzu-Ping ^{[4
]}

Shao, Weilan ^{[3
]}

Guo, Rey-Ting ^{[2
]}

机构：

[1] Tianjin Univ Sci & Technol, Coll Biotechnol, Tianjin 300457, Peoples R China

[2] Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Ind Enzymes Natl Engn Lab, Tianjin 300308, Peoples R China

[3] Jiangsu Univ, Sch Environm, Biofuels Inst, Zhenjiang 212013, Peoples R China

[4] Acad Sinica, Inst Biol Chem, Taipei 115, Taiwan

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2014年 / 70卷

基金：

中国国家自然科学基金;

关键词：

L-HOMOCYSTEINE HYDROLASE; SITE-DIRECTED MUTAGENESIS; CRYSTAL-STRUCTURE; PLASMODIUM-FALCIPARUM; CATALYTIC MECHANISM; INHIBITORS; ERITADENINE; ANALOGS; CLONING; LIVER;

D O I：

10.1107/S2053230X14013478

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

S-Adenosylhomocysteine hydrolase (SAHH) catalyzes the reversible conversion of S-adenosylhomocysteine into adenosine and homocysteine. The SAHH from Thermotoga maritima (TmSAHH) was expressed in Escherichia coli and the recombinant protein was purified and crystallized. TmSAHH crystals belonging to space group C2, with unit-cell parameters a = 106.3, b = 112.0, c = 164.9 angstrom, beta = 103.5 degrees, were obtained by the sitting-drop vapour-diffusion method and diffracted to 2.85 angstrom resolution. Initial phase determination by molecular replacement clearly indicated that the crystal contains one homotetramer per asymmetric unit. Further refinement of the crystal structure is in progress.

引用

页码：1563 / 1565

页数：3

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