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人源MAWDBP(一种类似吩嗪生物合成蛋白家族的成员)的纯化、结晶及初步结构表征

The purification, crystallization and preliminary structural characterization of human MAWDBP, a member of the phenazine biosynthesis-like protein family.

作者信息

Herde Petra, Blankenfeldt Wulf

机构信息

Max-Planck-Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt 6):546-9. doi: 10.1107/S1744309106015648. Epub 2006 May 31.

DOI:10.1107/S1744309106015648
PMID:16754977
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2243103/
Abstract

MAWDBP is the only representative of the phenazine biosynthesis-like protein family in the human genome. Its expression is elevated in several disease processes, including insulin resistance, folate deficiency and hypotension, and it may also be involved in carcinogenesis. The exact molecular function of MAWDBP is unknown. Native and seleno-L-methionine-labelled MAWDBP were expressed in Escherichia coli and crystallized at room temperature from precipitants containing 10 mM KF, 14%(w/v) PEG 3350 and 0.1 M sodium citrate pH 5.4. Crystals belong to space group H32, with unit-cell parameters a = b = 187, c = 241 A, indicative of three to five monomers per asymmetric unit. Crystals were cryoprotected with 15%(v/v) glycerol and data have been collected to 2.7 A resolution.

摘要

MAWDBP是人类基因组中吩嗪生物合成样蛋白家族的唯一代表。它在包括胰岛素抵抗、叶酸缺乏和低血压在内的多种疾病过程中表达升高,并且可能也参与致癌作用。MAWDBP的确切分子功能尚不清楚。天然的和硒代-L-甲硫氨酸标记的MAWDBP在大肠杆菌中表达,并在室温下从含有10 mM KF、14%(w/v)PEG 3350和0.1 M柠檬酸钠pH 5.4的沉淀剂中结晶。晶体属于空间群H32,晶胞参数a = b = 187,c = 241 Å,表明每个不对称单元中有三到五个单体。晶体用15%(v/v)甘油进行冷冻保护,并且数据已收集至2.7 Å分辨率。