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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.

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.

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