Iron sulfur proteins
From Proteopedia
(Difference between revisions)
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==4Fe–4S clusters== | ==4Fe–4S clusters== | ||
===4-hydroxy-2-methylbut-2-enyl diphosphate reductase=== | ===4-hydroxy-2-methylbut-2-enyl diphosphate reductase=== | ||
| - | + | 4-hydroxy-2-methylbut-2-enyl diphosphate reductase (IspH or HMBPP reductase) is an <scene name='59/595217/Cv/3'>iron-sulfur</scene> containing protein. IspH converts 1-hydroxy-2-methylbut-2-enyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). IspH participates in isoprenoid biosynthesis. IspH is the last enzyme in the nonmevalonate pathway. <ref>PMID:19035630</ref> IspH is involved in penicillin tolerance. | |
*<scene name='59/595217/Cv/8'>E. coli Fe4S4-containing IspH complex with HMBPP</scene> is shown. | *<scene name='59/595217/Cv/8'>E. coli Fe4S4-containing IspH complex with HMBPP</scene> is shown. | ||
*<scene name='59/595217/Cv/9'>Fe4S4 binding site</scene>. | *<scene name='59/595217/Cv/9'>Fe4S4 binding site</scene>. | ||
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===Acetyl-CoA synthase IV subunit α from ''Carboxydothermus hydrogenoformans''=== | ===Acetyl-CoA synthase IV subunit α from ''Carboxydothermus hydrogenoformans''=== | ||
| - | + | <scene name='49/492892/Cv/11'>Fe4S4 center and 2 Ni+2 ions form interactions with 6 cysteine residues</scene> in Acetyl-CoA synthase IV subunit α from ''Carboxydothermus hydrogenoformans'' ([[1ru3]]).<ref>PMID:14699043</ref> Water molecules shown as red spheres. | |
</StructureSection> | </StructureSection> | ||
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 14:55, 28 October 2019
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References
- ↑ Rekittke I, Wiesner J, Rohrich R, Demmer U, Warkentin E, Xu W, Troschke K, Hintz M, No JH, Duin EC, Oldfield E, Jomaa H, Ermler U. Structure of (E)-4-hydroxy-3-methyl-but-2-enyl diphosphate reductase, the terminal enzyme of the non-mevalonate pathway. J Am Chem Soc. 2008 Dec 24;130(51):17206-7. PMID:19035630 doi:http://dx.doi.org/10.1021/ja806668q
- ↑ Span I, Grawert T, Bacher A, Eisenreich W, Groll M. Crystal Structures of Mutant IspH Proteins Reveal a Rotation of the Substrate's Hydroxymethyl Group during Catalysis. J Mol Biol. 2011 Nov 23. PMID:22137895 doi:10.1016/j.jmb.2011.11.033
- ↑ Svetlitchnyi V, Dobbek H, Meyer-Klaucke W, Meins T, Thiele B, Romer P, Huber R, Meyer O. A functional Ni-Ni-[4Fe-4S] cluster in the monomeric acetyl-CoA synthase from Carboxydothermus hydrogenoformans. Proc Natl Acad Sci U S A. 2004 Jan 13;101(2):446-51. Epub 2003 Dec 29. PMID:14699043 doi:10.1073/pnas.0304262101
