Crystallization and preliminary X-ray diffraction analysis of brefeldin A-ADP ribosylated substrate (BARS).

Nardini M; Spano S; Cericola CPesce ADamonte GLuini ACorda DBolognesi M

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Crystallization and preliminary X-ray diffraction analysis of brefeldin A-ADP ribosylated substrate (BARS).

机译：结晶和初步的x射线衍射分析brefeldin A-ADP ribosylated衬底(酒吧)。

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Brefeldin A-ADP ribosylated substrate (BARS) is a newly discovered enzyme involved in membrane fission, catalyzing the formation of phosphatidic acid by transfer of an acyl group from acyl-CoA to lysophosphatidic acid. A truncated form of BARS, lacking the C-terminal segment expected to interact with the Golgi membrane, has been expressed in soluble form in Escherichia coli, purified and crystallized. BARS crystals diffract up to 2.5 A resolution using synchrotron radiation and belong to space group P6(2)22/P6(4)22, with unit-cell parameters a = b = 89.2, c = 162.6 A, alpha = beta = 90, gamma = 120 degrees and one molecule (39.5 kDa) per asymmetric unit. SeMet-substituted BARS has been crystallized under growth conditions very similar to those of the native protein.

机译：Brefeldin A-ADP ribosylated衬底(酒吧)新发现的酶参与了膜裂变,催化磷脂的形成酸通过转让一个酰基酰coalysophosphatidic酸。酒吧,缺乏将c端部分与高尔基体膜,交互以可溶性形式表达在大肠杆菌中,纯化和结晶。2.5使用同步解决辐射和属于空间群P6 (2) 22 / P6(4) 22日,晶胞参数a = b= 89.2, c = 162.6,α=β= 90,γ=120度,一个分子(39.5 kDa)不对称单元。结晶生长条件下非常相似本机的蛋白质。

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《Acta crystallographica.Section D. Biological crystallography》 |2002年第2期|1068-1070|共3页
作者
Nardini M; Spano S; Cericola CPesce ADamonte GLuini ACorda DBolognesi M;
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Department of Physics and INFM, University of Genova c/o Advanced Biotechnology Center, Largo Rosanna Benzi 10, 16132 Genova, Italy.;

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正文语种英语
中图分类化学;
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Escherichia coli; Carrier Proteins; brefeldinBrefeldin Agolgi membranePhosphatidic acidsBinding ProteinX-ray diffraction analysisacyl groupCrystallization;

机译：大肠杆菌;承运人membranePhosphatidic acidsBinding ProteinX-ray衍射analysisacyl groupCrystallization;

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Crystallization and preliminary X-ray diffraction analysis of brefeldin A-ADP ribosylated substrate (BARS).

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