STAFF PRIORITY TIME CRYSTAL STRUCTURE DETERMINATION OF PNGASE F
STAFF PRIORITY TIME CRYSTAL STRUCTURE DETERMINATION OF PNGASE F
批准号:
6437416
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:
2001
资助国家:
美国
项目状态:
已结题
起止时间:
2001-03-01 至 2002-02-28
中文摘要
肽-N4-(N-乙酰基-b-D-葡糖胺基)天冬酰胺酰胺酶F是一种
来自脑膜败血黄杆菌的34 kDa氨基水解酶,其去除
来自糖蛋白的完整天冬酰胺连接的寡糖。 高
分辨率晶体学数据(1.6 E及更好)收集于
三种突变体和与产物复合的天然酶,
二-N-乙酰壳二糖 该模型目前正在完善,
数据集。 所有模型的R因子都在18%左右。 高
解析结构显示了酶结合的清晰细节,
其产品,并提供新的起点,设计进一步
实验旨在研究酶的作用机理。
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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