Iron sulfur proteins
From Proteopedia
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<StructureSection load='' size='400' side='right' scene='82/827883/Cv/2' caption=''> | <StructureSection load='' size='400' side='right' scene='82/827883/Cv/2' caption=''> | ||
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===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. | 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='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. | <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. | ||
| - | === Crystal structures of the all cysteinyl coordinated D14C variant of ''Pyrococcus furiosus'' ferredoxin: [4Fe-4S] <-> [3Fe-4S] cluster conversion | + | === Crystal structures of the all cysteinyl coordinated D14C variant of ''Pyrococcus furiosus'' ferredoxin: [4Fe-4S] <-> [3Fe-4S] cluster conversion<ref>DOI 10.1007/s00775-011-0778-7</ref> === |
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Structures of the all cysteinyl coordinated D14C variant of ferredoxin from the hyperthermophilic archaeon ''Pyrococcus furiosus'' have been determined for the <scene name='Journal:JBIC:10/Cv1/5'>[4Fe-4S]</scene> <-> and <scene name='Journal:JBIC:10/Cv1/6'>[3Fe-4S]</scene> forms (<scene name='Journal:JBIC:10/Cv1/8'>click to enlarge</scene>). The [4Fe-4S] form diffracted to 1.7 Å and two different types of molecules were found in the crystal ([[2z8q]]). They have different crystal packing and intramolecular disulfide bond conformation. The crystal packing reveals a <scene name='Journal:JBIC:10/Cv/5'>beta-sheet interaction between A molecules</scene> (shown in <font color='blue'><b>blue</b></font> and <span style="color:green;background-color:black;font-weight:bold;">green</span>) in adjacent asymmetric units, while <scene name='Journal:JBIC:10/Cv/6'>B molecules are packed as monomers in a less rigid position next to the A-A extended beta-sheet dimers</scene> (shown in <font color='red'><b>red</b></font> and <span style="color:yellow;background-color:black;font-weight:bold;">yellow</span>). The <scene name='Journal:JBIC:10/Cv1/9'>intramolecular disulfide bond in the A molecules is in a double conformation</scene> while the intramolecular disulfide bond in the <scene name='Journal:JBIC:10/Cv1/10'>B molecules is in a single conformation</scene> (<scene name='Journal:JBIC:10/Cv1/11'>click to see morph</scene>, molecule A is shown in <font color='blue'><b>blue</b></font> and molecule B in <span style="color:green;background-color:black;font-weight:bold;">green</span>). | Structures of the all cysteinyl coordinated D14C variant of ferredoxin from the hyperthermophilic archaeon ''Pyrococcus furiosus'' have been determined for the <scene name='Journal:JBIC:10/Cv1/5'>[4Fe-4S]</scene> <-> and <scene name='Journal:JBIC:10/Cv1/6'>[3Fe-4S]</scene> forms (<scene name='Journal:JBIC:10/Cv1/8'>click to enlarge</scene>). The [4Fe-4S] form diffracted to 1.7 Å and two different types of molecules were found in the crystal ([[2z8q]]). They have different crystal packing and intramolecular disulfide bond conformation. The crystal packing reveals a <scene name='Journal:JBIC:10/Cv/5'>beta-sheet interaction between A molecules</scene> (shown in <font color='blue'><b>blue</b></font> and <span style="color:green;background-color:black;font-weight:bold;">green</span>) in adjacent asymmetric units, while <scene name='Journal:JBIC:10/Cv/6'>B molecules are packed as monomers in a less rigid position next to the A-A extended beta-sheet dimers</scene> (shown in <font color='red'><b>red</b></font> and <span style="color:yellow;background-color:black;font-weight:bold;">yellow</span>). The <scene name='Journal:JBIC:10/Cv1/9'>intramolecular disulfide bond in the A molecules is in a double conformation</scene> while the intramolecular disulfide bond in the <scene name='Journal:JBIC:10/Cv1/10'>B molecules is in a single conformation</scene> (<scene name='Journal:JBIC:10/Cv1/11'>click to see morph</scene>, molecule A is shown in <font color='blue'><b>blue</b></font> and molecule B in <span style="color:green;background-color:black;font-weight:bold;">green</span>). | ||
Revision as of 13:22, 29 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
- ↑ Lovgreen MN, Martic M, Windahl MS, Christensen HE, Harris P. Crystal structures of the all-cysteinyl-coordinated D14C variant of Pyrococcus furiosus ferredoxin: [4Fe-4S] <--> [3Fe-4S] cluster conversion. J Biol Inorg Chem. 2011 Apr 12. PMID:21484348 doi:10.1007/s00775-011-0778-7
