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3f7t

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Current revision (00:29, 28 December 2023) (edit) (undo)
 
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<StructureSection load='3f7t' size='340' side='right'caption='[[3f7t]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3f7t' size='340' side='right'caption='[[3f7t]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[3f7t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. 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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<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>
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<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>
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<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>
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<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>
<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 ==
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[[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>
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[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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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]]
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[[Category: Escherichia coli K-12]]
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[[Category: Ecoli]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bacher, A]]
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[[Category: Bacher A]]
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[[Category: Eisenreich, W]]
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[[Category: Eisenreich W]]
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[[Category: Eppinger, J]]
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[[Category: Eppinger J]]
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[[Category: Graewert, T]]
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[[Category: Graewert T]]
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[[Category: Groll, M]]
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[[Category: Groll M]]
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[[Category: Rohdich, F]]
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[[Category: Rohdich F]]
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[[Category: Iron]]
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[[Category: Iron-sulfur]]
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[[Category: Isoprene biosynthesis]]
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[[Category: Metal-binding]]
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[[Category: Nadp]]
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[[Category: Oxidoreductase]]
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[[Category: Protein binding]]
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[[Category: Pseudo-c3-symmetry]]
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[[Category: Unprecedent fold for fes-cluster protein]]
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Current revision

Structure of active IspH shows a novel fold with a [3Fe-4S] cluster in the catalytic centre

PDB ID 3f7t

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OCA

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