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 [ | + | <table><tr><td colspan='2'>[[3f7t]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/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" id="ligandDat"><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 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0029, ispH, JW0027, lytB, yaaE ([https://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'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/4-hydroxy-3-methylbut-2-enyl_diphosphate_reductase 4-hydroxy-3-methylbut-2-enyl diphosphate reductase], with EC number [https://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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3f7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f7t OCA], [https://pdbe.org/3f7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f7t RCSB], [https://www.ebi.ac.uk/pdbsum/3f7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f7t ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/ISPH_ECOLI ISPH_ECOLI]] Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is also involved in penicillin tolerance and control of the stringent response. Seems to directly or indirectly interact with RelA to maintain it in an inactive form during normal growth.<ref>PMID:19569147</ref> <ref>PMID:20080550</ref> <ref>PMID:22137895</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
- | *[[4-hydroxy-3-methylbut-2-enyl diphosphate reductase|4-hydroxy-3-methylbut-2-enyl diphosphate reductase]] | + | *[[4-hydroxy-3-methylbut-2-enyl diphosphate reductase 3D structures|4-hydroxy-3-methylbut-2-enyl diphosphate reductase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]] | [[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]] | ||
[[Category: Ecoli]] | [[Category: Ecoli]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Bacher, A]] | [[Category: Bacher, A]] | ||
[[Category: Eisenreich, W]] | [[Category: Eisenreich, W]] |
Revision as of 09:26, 23 February 2022
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 | Large Structures | 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