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IspG

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== Structural highlights ==
== Structural highlights ==
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The substrate <scene name='77/774679/Cv/2'>MEcPP is located in the cavity between the TIM-barrel and the lid domain</scene> of IpsG. <scene name='77/774679/Cv/3'>It binds covalently to the 4Fe4S cluster</scene> and its <scene name='77/774679/Cv/8'>PP moiety binds to 4 Arg and 1 Lys sidechains</scene><ref>PMID:22967895</ref>.
+
The substrate <scene name='77/774679/Cv/2'>MEcPP is located in the cavity between the TIM-barrel and the lid domain</scene> of IpsG. <scene name='77/774679/Cv/3'>It binds covalently to the 4Fe4S cluster</scene> and its <scene name='77/774679/Cv/8'>PP moiety binds to 4 Arg and 1 Lys sidechains</scene>.
*<scene name='77/774679/Cv/6'>4Fe4S cluster binding site</scene>.
*<scene name='77/774679/Cv/6'>4Fe4S cluster binding site</scene>.
*<scene name='77/774679/Cv/7'>Whole active site</scene>.
*<scene name='77/774679/Cv/7'>Whole active site</scene>.
 +
*<scene name='77/774679/Cv/9'>1st Cl coordination site</scene>.
 +
*<scene name='77/774679/Cv/10'>Cl/K cluster coordination site</scene>.
</StructureSection>
</StructureSection>
== 3D Structures of IspG ==
== 3D Structures of IspG ==

Revision as of 13:15, 30 November 2017

IspG containing 4Fe4S cluster complex with MEcPP, MES, K+ (purple) and Cl- (green) ions (PDB entry 4g9p)

Drag the structure with the mouse to rotate

3D Structures of IspG

Updated on 30-November-2017

3noy – IspG – Aquifex aeolicus
4mwa – IspG – Bacillus anthracis
2y0f – TtIspG – Thermus thermophilus
4s38, 4g9p – TtIspG + MEcPP
4s39, 4s23 – TtIspG + HMBPP
4s3a, 4s3b, 4s3c – TtIspG + intermediate
4s3c – TtIspG + PPi
4s3e, 4s3f – TtIspG + inhibitor

References

  1. ↑ Lee M, Grawert T, Quitterer F, Rohdich F, Eppinger J, Eisenreich W, Bacher A, Groll M. Biosynthesis of Isoprenoids: Crystal Structure of the [4Fe-4S] Cluster Protein IspG. J Mol Biol. 2010 Oct 7. PMID:20932974 doi:10.1016/j.jmb.2010.09.050
  2. ↑ Liu YL, Guerra F, Wang K, Wang W, Li J, Huang C, Zhu W, Houlihan K, Li Z, Zhang Y, Nair SK, Oldfield E. Structure, function and inhibition of the two- and three-domain 4Fe-4S IspG proteins. Proc Natl Acad Sci U S A. 2012 May 29;109(22):8558-63. doi:, 10.1073/pnas.1121107109. Epub 2012 May 14. PMID:22586085 doi:http://dx.doi.org/10.1073/pnas.1121107109

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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