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Crystallization and preliminary crystallographic studies of 3‐deoxy‐D‐ manno ‐octulosonate‐8‐phosphate synthase from Escherichia coli
Author(s) -
Tolbert William D.,
Moll Jonathan R.,
Bauerle Ronald,
Kretsinger Robert H.
Publication year - 1996
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199603)24:3<407::aid-prot16>3.0.co;2-q
Subject(s) - atp synthase , crystallization , phosphate , phosphoenolpyruvate carboxykinase , chemistry , enzyme , crystallography , biochemistry , stereochemistry , organic chemistry
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 Å and the other with a = b = c = 233 Å.