DAHP synthase
From Proteopedia
(Difference between revisions)
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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/7'>substrate (PEP)</scene>, <scene name='70/708806/Cv/8'>inhibitor (phenylalanine)</scene> and <scene name='70/708806/Cv/9'>metal ion (Mn+2)</scene> are seen. The bivalent metal is bound to a Cys-X-X-His motif.<ref>PMID:12126632</ref> | The DAHPS active site is located in a channel at the C-terminal of the enzyme where the <scene name='70/708806/Cv/7'>substrate (PEP)</scene>, <scene name='70/708806/Cv/8'>inhibitor (phenylalanine)</scene> and <scene name='70/708806/Cv/9'>metal ion (Mn+2)</scene> are seen. The bivalent metal is bound to a Cys-X-X-His motif.<ref>PMID:12126632</ref> | ||
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| + | == 3D Structures of DAHP synthase == | ||
| + | [[DAHP synthase 3D structures]] | ||
</StructureSection> | </StructureSection> | ||
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**[[4ixx]] - NmDAHPS (mutant) + Mn <br /> | **[[4ixx]] - NmDAHPS (mutant) + Mn <br /> | ||
**[[3tqk]] - DAHPS + Mn – ''Francisella tularensis''<br /> | **[[3tqk]] - DAHPS + Mn – ''Francisella tularensis''<br /> | ||
| + | **[[3nvt]] - LmDAHPS + Mn – ''Listeria monocytogenes''<br /> | ||
*DAHP synthase binary complex | *DAHP synthase binary complex | ||
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**[[2w19]] - MtDAHPS + chorismate mutase <br /> | **[[2w19]] - MtDAHPS + chorismate mutase <br /> | ||
**[[5huc]] - CgDAHPS + Mn + PEP – ''Corynebacterium glutamicum''<br /> | **[[5huc]] - CgDAHPS + Mn + PEP – ''Corynebacterium glutamicum''<br /> | ||
| + | **[[3tfc]] - LmDAHPS + Mn + PEP <br /> | ||
*DAHP synthase higher complex | *DAHP synthase higher complex | ||
Revision as of 08:57, 3 June 2019
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3D Structures of DAHP synthase
Updated on 03-June-2019
References
- ↑ 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
- ↑ 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
