Iron sulfur proteins

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(New page: <StructureSection load='' size='450' side='right' scene='82/827883/Cv/2' caption=''> ==4Fe–4S clusters== *<scene name='49/492892/Cv/11'>Fe4S4 center and 2 Ni+2 ions form interactions wi...)
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<StructureSection load='' size='450' side='right' scene='82/827883/Cv/2' caption=''>
<StructureSection load='' size='450' side='right' scene='82/827883/Cv/2' caption=''>
==4Fe–4S clusters==
==4Fe–4S clusters==
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===4-hydroxy-2-methylbut-2-enyl diphosphate reductase===
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'''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.
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*<scene name='59/595217/Cv/8'>E. coli Fe4S4-containing IspH complex with HMBPP</scene> is shown.
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*<scene name='59/595217/Cv/9'>Fe4S4 binding site</scene>.
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*Of note, <scene name='59/595217/Cv/12'>there are very interesting interactions between iron atoms of Fe4S4 and sulfur atoms of 3 Cys residues</scene>.
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*<scene name='59/595217/Cv/14'>The 4th iron atom of Fe4S4 interacts with substrate HMBPP</scene>.
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*<scene name='59/595217/Cv/16'>HMBPP binding site</scene>. Water molecules are shown as red spheres.
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*<scene name='59/595217/Cv/17'>Whole active site</scene> (PDB code [[3szl]]).<ref>PMID:22137895</ref>
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*<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.
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===Acetyl-CoA synthase IV subunit α from ''Carboxydothermus hydrogenoformans''===
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*<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 14:53, 28 October 2019

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References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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

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