MECDP synthase
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<scene name='52/526157/Cv/7'>MECPS active site is located in a cleft between 2 subunits</scene> and contains the <scene name='52/526157/Cv/8'>metal ions</scene><ref>PMID:11997478</ref>. Water molecules are shown as red spheres. | <scene name='52/526157/Cv/7'>MECPS active site is located in a cleft between 2 subunits</scene> and contains the <scene name='52/526157/Cv/8'>metal ions</scene><ref>PMID:11997478</ref>. Water molecules are shown as red spheres. | ||
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==3D structures of MECDP synthase== | ==3D structures of MECDP synthase== | ||
+ | [[MECDP synthase 3D structures]] | ||
- | + | </StructureSection> | |
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- | **[[3p0z]], [[3qhd]] - BpMECPS + imidazo derivative + pyrimidine derivative + cytidine + Zn<br /> | ||
- | **[[1h48]] - EcMECPS + MECP + CMP + geranyl diphosphate + Mn + Zn<br /> | ||
- | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Current revision
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References
- ↑ Richard SB, Ferrer JL, Bowman ME, Lillo AM, Tetzlaff CN, Cane DE, Noel JP. Structure and mechanism of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase. An enzyme in the mevalonate-independent isoprenoid biosynthetic pathway. J Biol Chem. 2002 Mar 8;277(10):8667-72. Epub 2002 Jan 10. PMID:11786530 doi:http://dx.doi.org/10.1074/jbc.C100739200
- ↑ Kishida H, Wada T, Unzai S, Kuzuyama T, Takagi M, Terada T, Shirouzu M, Yokoyama S, Tame JR, Park SY. Structure and catalytic mechanism of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (MECDP) synthase, an enzyme in the non-mevalonate pathway of isoprenoid synthesis. Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):23-31. Epub 2002, Dec 19. PMID:12499535
- ↑ Kemp LE, Bond CS, Hunter WN. Structure of 2C-methyl-D-erythritol 2,4- cyclodiphosphate synthase: an essential enzyme for isoprenoid biosynthesis and target for antimicrobial drug development. Proc Natl Acad Sci U S A. 2002 May 14;99(10):6591-6. Epub 2002 May 7. PMID:11997478 doi:10.1073/pnas.102679799