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

✍ Scribed by Tolbert, William D.; Moll, Jonathan R.; Bauerle, Ronald; Kretsinger, Robert H.

Publisher: John Wiley and Sons
Year: 1996
Tongue: English
Weight: 221 KB
Volume: 24
Category: Article
ISSN: 0887-3585
DOI: 10.1002/(sici)1097-0134(199603)24:3<407::aid-prot16>3.0.co;2-q

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✦ Synopsis

3-Deoxy-D-manm-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. 59129-170,1990). We have crystallized two forms of KDOP synthase belonging to space groups I23 or I2,3, one with a = b = c = 118.0 A and the other with a = b = c = 233 A.

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