Kdo-8-phosphate synthase

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== Structural highlights ==
== Structural highlights ==
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The biological assembly of Metallo Kdo-8-phosphate synthase from ''Neisseria meningitidis'' is <scene name='52/525184/Cv/3'>homotetramer</scene>. The <scene name='52/525184/Cv/6'>active site of the metallo KPS contains a divalent cation and the PEP substrate</scene><ref>PMID:19447118</ref>. Water molecules shown as red spheres.
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The biological assembly of Metallo Kdo-8-phosphate synthase from ''Neisseria meningitidis'' is <scene name='52/525184/Cv/7'>homotetramer</scene>. The <scene name='52/525184/Cv/8'>active site of the metallo KPS contains a divalent cation and the PEP substrate</scene><ref>PMID:19447118</ref>. Water molecules shown as red spheres.
</StructureSection>
</StructureSection>
==3D structures of Kdo-8-phosphate synthase==
==3D structures of Kdo-8-phosphate synthase==

Revision as of 10:40, 1 July 2019

Metallo Kdo-8-phosphate synthase tetramer complex with phosphoenolpyruvate, glycerol, Cl- (green), Na+ (large purple) and Mn+2 (small purple) ion, 3fyp

Drag the structure with the mouse to rotate

3D structures of Kdo-8-phosphate synthase

Updated on 01-July-2019

References

  1. ↑ Krosky DJ, Alm R, Berg M, Carmel G, Tummino PJ, Xu B, Yang W. Helicobacter pylori 3-deoxy-D-manno-octulosonate-8-phosphate (KDO-8-P) synthase is a zinc-metalloenzyme. Biochim Biophys Acta. 2002 Feb 11;1594(2):297-306. PMID:11904225
  2. ↑ Cochrane FC, Cookson TV, Jameson GB, Parker EJ. Reversing evolution: re-establishing obligate metal ion dependence in a metal-independent KDO8P synthase. J Mol Biol. 2009 Jul 24;390(4):646-61. Epub 2009 May 15. PMID:19447118 doi:10.1016/j.jmb.2009.05.014

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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