title: Crystallization and preliminary crystallographic studies of 3-deoxy-D-manno-octulosonate-8-phosphate synthase from Escherichia coli.
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.
authors.affiliation: Department of Biology, University of Virginia, Charlottesville 22903, USA.
authors.forename: W D
authors.initials: WD
authors.lastname: Tolbert
authors.forename: J R
authors.initials: JR
authors.lastname: Moll
authors.forename: R
authors.initials: R
authors.lastname: Bauerle
authors.forename: R H
authors.initials: RH
authors.lastname: Kretsinger
mesh_terms: D000446:Aldehyde-Lyases / Q000737:chemistry / Q000302:isolation & purification*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*
chemical_list: C020011:2-dehydro-3-deoxyphosphooctonate aldolase; D000446:Aldehyde-Lyases