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来自大肠杆菌的3-脱氧-D-甘露糖辛酮酸酯-8-磷酸合酶的结晶及初步晶体学研究

Crystallization and preliminary crystallographic studies of 3-deoxy-D-manno-octulosonate-8-phosphate synthase from Escherichia coli.

作者信息

Tolbert W D, Moll J R, Bauerle R, Kretsinger R H

机构信息

Department of Biology, University of Virginia, Charlottesville 22903, USA.

出版信息

Proteins. 1996 Mar;24(3):407-8. doi: 10.1002/(SICI)1097-0134(199603)24:3<407::AID-PROT16>3.0.CO;2-Q.

DOI:10.1002/(SICI)1097-0134(199603)24:3<407::AID-PROT16>3.0.CO;2-Q
PMID:8778790
Abstract

3-Deoxy-D-manno-octulosonate-8-phosphate (KDOP) synthase catalyzes the production of KDOP from phosphoenolpyruvate (PEP) and arabinose-5-phosphate (A5P). In gram-negative bacteria KDOP is subsequently dephosphorylated, cytidylylated, and linked to lipid A and is required for lipid A incorporation into the outer membrane (Raetz, Annu. Rev. Biochem. 59:129-170, 1990). We have crystallized two forms of KDOP synthase belonging to space groups I23 or I2(1)3, one with a = b = c = 118.0 A and the other with a = b = c = 233 A.

摘要

3-脱氧-D-甘露-辛酮糖酸-8-磷酸(KDOP)合酶催化由磷酸烯醇丙酮酸(PEP)和阿拉伯糖-5-磷酸(A5P)生成KDOP。在革兰氏阴性菌中,KDOP随后会被去磷酸化、胞苷酰化,并与脂多糖A连接,这是脂多糖A整合到外膜所必需的(雷茨,《生物化学年度评论》59:129 - 170,1990年)。我们已经结晶出属于I23或I2(1)3空间群的两种形式的KDOP合酶,一种的a = b = c = 118.0埃,另一种的a = b = c = 233埃。

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