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Crystallization and preliminary crystallographic studies of 3-deoxy-D-manno-octulosonate-8-phosphate synthase from Escherichia coli.
Tolbert, W D; Moll, J R; Bauerle, R; Kretsinger, R H.
Affiliation
  • Tolbert WD; Department of Biology, University of Virginia, Charlottesville 22903, USA.
Proteins ; 24(3): 407-8, 1996 Mar.
Article in En | MEDLINE | ID: mdl-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. 59129-170, 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.
Subject(s)
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Collection: 01-internacional Database: MEDLINE Main subject: Aldehyde-Lyases / Escherichia coli Language: En Journal: Proteins Journal subject: BIOQUIMICA Year: 1996 Document type: Article Affiliation country: United States
Search on Google
Collection: 01-internacional Database: MEDLINE Main subject: Aldehyde-Lyases / Escherichia coli Language: En Journal: Proteins Journal subject: BIOQUIMICA Year: 1996 Document type: Article Affiliation country: United States