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

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Aldehyde-Lyases / chemistry
  • Aldehyde-Lyases / isolation & purification*
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / enzymology*

Substances

  • 2-dehydro-3-deoxyphosphooctonate aldolase
  • Aldehyde-Lyases