4h4e

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'''Unreleased structure'''
 
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The entry 4h4e is ON HOLD
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==IspH in complex with (E)-4-mercapto-3-methylbut-2-enyl diphosphate==
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<StructureSection load='4h4e' size='340' side='right'caption='[[4h4e]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4h4e]] 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=4H4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H4E FirstGlance]. <br>
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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]] 1.7&#8491;</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=10G:(2E)-3-METHYL-4-SULFANYLBUT-2-EN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>10G</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></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=4h4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h4e OCA], [https://pdbe.org/4h4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h4e RCSB], [https://www.ebi.ac.uk/pdbsum/4h4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h4e ProSAT]</span></td></tr>
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</table>
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== 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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The iron-sulfur protein IspH catalyzes a key step in isoprenoid biosynthesis in bacteria and malaria parasites. Crystal structures of IspH complexed with three substrate analogues reveal their mode of binding and suggest new routes to inhibitor design.
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Authors: Span, I., Eisenreich, W., Jauch, J., Bacher, A., Groll, M.
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Structures of Fluoro, Amino, and Thiol Inhibitors Bound to the [Fe(4) S(4) ] Protein IspH.,Span I, Wang K, Wang W, Jauch J, Eisenreich W, Bacher A, Oldfield E, Groll M Angew Chem Int Ed Engl. 2013 Jan 10. doi: 10.1002/anie.201208469. PMID:23307751<ref>PMID:23307751</ref>
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Description: IspH in complex with (E)-4-mercapto-3-methylbut-2-enyl diphosphate
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4h4e" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[4-hydroxy-3-methylbut-2-enyl diphosphate reductase 3D structures|4-hydroxy-3-methylbut-2-enyl diphosphate reductase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli K-12]]
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[[Category: Large Structures]]
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[[Category: Bacher A]]
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[[Category: Eisenreich W]]
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[[Category: Groll M]]
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[[Category: Jauch J]]
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[[Category: Span I]]

Current revision

IspH in complex with (E)-4-mercapto-3-methylbut-2-enyl diphosphate

PDB ID 4h4e

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