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学科主题: 生命有机化学
题名: Crystallographic analysis of NosA, which catalyzes terminal amide formation in the biosynthesis of nosiheptide
其他题名: 硫肽nosiheptide生物合成最后一般碳酰胺化被NosA催化形成的晶体学研究
作者: Wang YT(王彦婷)1; Liu SS(刘珊珊)1; Me PF(么鹏飞)1; Yu Y(虞沂)1; Zhang Y(张岩)1; Lan WX(蓝文贤)1; Wang CX(王春喜)1; Ding JP(丁建平)1; Liu W(刘文)1; Cao CY(曹春阳)1
通讯作者: 曹春阳
刊名: Acta Crystallogr. F-Struct. Biol. Commun.
发表日期: 2015
DOI: 10.1107/S2053230X15011085
卷: 71, 页:1033-1037
收录类别: SCI
文章类型: 论文
英文摘要: Nosiheptide is a member of the thiopeptide family of antibiotics which demonstrates potent activities against various bacterial pathogens. The formation of its C-terminal amide is catalysed by NosA in an unusual strategy for maturating certain thiopeptides by processing precursor peptides featuring a serine extension. Here, a recombinant C-terminally truncated selenomethionine-derivatized NosA(1-111) variant from Streptomyces actuosus consisting of residues 1-111, named SeMet NosA(1-111), was crystallized using the sitting-drop vapour-diffusion method. Diffraction data were collected to 2.40 angstrom resolution using synchrotron radiation. The crystals belonged to the primitive cubic space group P4(1)32, with unit-cell parameters a = b = c = 143.3 angstrom. Assuming the presence of three molecules in the asymmetric unit, the calculated Matthews coefficient was 3.94 angstrom(3)Da(-1) and the corresponding solvent content was 40.3%.
语种: 英语
相关网址: 查看原文
WOS记录号: WOS:000359352700019
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内容类型: 期刊论文
URI标识: http://ir.sioc.ac.cn/handle/331003/39519
Appears in Collections:生命有机化学国家重点实验室_期刊论文

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作者单位: 1.华中科技大学
2.中科院上海有机化学研究所, 生命有机化学国家重点实验室
3.中科院上海有机化学研究所, 生物与化学交叉研究中心

Recommended Citation:
Wang YT,Liu SS,Me PF,et al. Crystallographic analysis of NosA, which catalyzes terminal amide formation in the biosynthesis of nosiheptide[J]. Acta Crystallogr. F-Struct. Biol. Commun.,2015,71:1033-1037.
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