Purification, crystallization and preliminary X-ray crystallographic analysis of the phosphatase domain (PA3346PD) of the response regulator PA3346 from Pseudomonas aeruginosa PAO1

被引：0
|
作者：
Chen, Li-Ying [1 ,2 ]
Wu, Pei-Hsun [2 ,3 ]
Guan, Hong-Hsiang [2 ]
Fun, Hoong-Kun [4 ,5 ]
Chang, Hwan-You [3 ]
Chen, Chun-Jung [1 ,2 ,4 ,6 ]
机构：
[1] Natl Cheng Kung Univ, Inst Biotechnol, Tainan 701, Taiwan
[2] Natl Synchrotron Radiat Res Ctr, Sci Res Div, Life Sci Grp, Hsinchu 30076, Taiwan
[3] Natl Tsing Hua Univ, Inst Mol Med, Hsinchu 30013, Taiwan
[4] King Saud Univ, Coll Pharm, Dept Pharmaceut Chem, Riyadh 11451, Saudi Arabia
[5] Univ Sains Malaysia, Sch Phys, Xray Crystallog Unit, Usm Pulau Pinang 11800, Malaysia
[6] Natl Tsing Hua Univ, Dept Phys, Hsinchu 30013, Taiwan
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2015年 / 71卷
关键词：
phosphatase domain; response regulator; Pseudomonas aeruginosa; SYSTEM; MOTILITY;
D O I：
10.1107/S2053230X15004197
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
The phosphatase domain (PA3346PD) of the response regulator PA3346 modulates the downstream anti-anti-sigma factor PA3347 to regulate swarming motility in Pseudomonas aeruginosa PAO1. PA3346PD, which comprises the protein phosphatase 2C domain (PP2C), is classified as a Ser/Thr phosphatase of the Mg2+- or Mn2+-dependent protein phosphatase (PPM) family. The recombinant PA3346PD, with molecular mass 26 kDa, was overexpressed in Escherichia coli, purified on an Ni2+-NTA agarose column and crystallized by the sitting-drop vapour-diffusion method. X-ray diffraction data were collected from PA3346PD crystals to a resolution of 2.58 angstrom and the crystals belonged to space group I4(1)32 or I4(3)32, with unit-cell parameter a = 157.61 angstrom. Preliminary analysis indicates the presence of a monomer of PA3346PD in the asymmetric unit with a solvent content of 58.4%.
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收藏
页码：434 / 437
页数：4
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