DAHP synthase

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== Structural highlights ==
== Structural highlights ==
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The <scene name='70/708806/Cv/3'>bivalent metal is bound to a Cys-X-X-His motif</scene>. The DAHPS active site is located in a channel at the C-terminal of the enzyme where the <scene name='70/708806/Cv/4'>substrate (PEP)</scene>, <scene name='70/708806/Cv/5'>inhibitor (phenylalanine)</scene> and the metal ion (Mn+2) are seen.<ref>PMID:12126632</ref>
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The DAHPS active site is located in a channel at the C-terminal of the enzyme where the <scene name='70/708806/Cv/4'>substrate (PEP)</scene>, <scene name='70/708806/Cv/5'>inhibitor (phenylalanine)</scene> and <scene name='70/708806/Cv/3'>metal ion (Mn+2)</scene> are seen. The bivalent metal is bound to a Cys-X-X-His motif.<ref>PMID:12126632</ref>
</StructureSection>
</StructureSection>

Revision as of 09:46, 28 December 2015

E. coli DAHP synthase complex with PEP, phenylalanine, sulfate and Mn+2 ion (PDB code 1kfl)

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3D Structures of DAHP synthase

Updated on 28-December-2015

References

  1. ↑ Stephens CM, Bauerle R. Analysis of the metal requirement of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli. J Biol Chem. 1991 Nov 5;266(31):20810-7. PMID:1682314
  2. ↑ Shumilin IA, Zhao C, Bauerle R, Kretsinger RH. Allosteric inhibition of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase alters the coordination of both substrates. J Mol Biol. 2002 Jul 26;320(5):1147-56. PMID:12126632

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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