STAFF PRIORITY TIME CRYSTAL STRUCTURE DETERMINATION OF PNGASE F
STAFF PRIORITY TIME CRYSTAL STRUCTURE DETERMINATION OF PNGASE F
批准号:
6658465
负责人:
PETER KUHN
金额:
$14.32万
依托单位:
依托单位国家:
美国
项目类别:
财政年份:
2002
资助国家:
美国
项目状态:
已结题
起止时间:
2002-03-01 至 2003-02-28
中文摘要
多肽-N4-(N-乙酰-b-D-氨基葡萄糖基)天冬酰胺酰胺酶F是一种
脑膜败血黄杆菌的34 kDa氨基水解酶
糖蛋白中完整的天冬酰胺连接的寡糖。高
分辨率晶体数据(1.6 E及更高)收集于
三个突变体和天然酶与产物形成复合体,
二-N-乙酰基壳二糖。该模型目前正在针对
数据集。所有模型的R因子都在18%左右。高潮
分辨结构显示了酶与其结合的清晰细节
并为其产品的进一步设计提供了新的起点
实验旨在探讨该酶的作用机理。
英文摘要
Peptide-N4-(N-acetyl-b-D-glucosaminyl) asparagine amidase F is a
34kDa aminohydrolase from Flavobacterium meningosepticum that removes
intact asparagine-linked oligosaccharides from glycoproteins. High
resolution crystallographic data (1.6 E and better) were collected on
three mutants and the native enzyme in complex with the product,
di-N-acetylchitobiose. The model is currently being refined against
the data sets. The R-factors of all models are around 18%. The high
resolution structures show clear details of binding of the enzyme to
its product and provide new starting points for the design of further
experiments aimed at the investigation of the mechanism of the enzyme.
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