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3f7t
From Proteopedia
(Difference between revisions)
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==Structure of active IspH shows a novel fold with a [3Fe-4S] cluster in the catalytic centre== | ==Structure of active IspH shows a novel fold with a [3Fe-4S] cluster in the catalytic centre== | ||
<StructureSection load='3f7t' size='340' side='right' caption='[[3f7t]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='3f7t' size='340' side='right' caption='[[3f7t]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3f7t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3f7t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F7T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3F7T FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0029, ispH, JW0027, lytB, yaaE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0029, ispH, JW0027, lytB, yaaE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> |
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-3-methylbut-2-enyl_diphosphate_reductase 4-hydroxy-3-methylbut-2-enyl diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.1.2 1.17.1.2] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-3-methylbut-2-enyl_diphosphate_reductase 4-hydroxy-3-methylbut-2-enyl diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.1.2 1.17.1.2] </span></td></tr> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3f7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f7t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3f7t RCSB], [http://www.ebi.ac.uk/pdbsum/3f7t PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3f7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f7t OCA], [http://pdbe.org/3f7t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3f7t RCSB], [http://www.ebi.ac.uk/pdbsum/3f7t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3f7t ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3f7t ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]] | [[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]] | ||
| - | [[Category: | + | [[Category: Ecoli]] |
[[Category: Bacher, A]] | [[Category: Bacher, A]] | ||
[[Category: Eisenreich, W]] | [[Category: Eisenreich, W]] | ||
Revision as of 06:41, 5 August 2016
Structure of active IspH shows a novel fold with a [3Fe-4S] cluster in the catalytic centre
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Categories: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | Ecoli | Bacher, A | Eisenreich, W | Eppinger, J | Graewert, T | Groll, M | Rohdich, F | Iron | Iron-sulfur | Isoprene biosynthesis | Metal-binding | Nadp | Oxidoreductase | Protein binding | Pseudo-c3-symmetry | Unprecedent fold for fes-cluster protein
