3uv6

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==Ec_IspH in complex with 4-hydroxybutyl diphosphate (1301)==
==Ec_IspH in complex with 4-hydroxybutyl diphosphate (1301)==
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<StructureSection load='3uv6' size='340' side='right' caption='[[3uv6]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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<StructureSection load='3uv6' size='340' side='right'caption='[[3uv6]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3uv6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UV6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UV6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3uv6]] 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=3UV6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UV6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0CH:4-HYDROXYBUTYL+TRIHYDROGEN+DIPHOSPHATE'>0CH</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 1.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ke8|3ke8]], [[3dnf|3dnf]], [[3urk|3urk]], [[3utc|3utc]], [[3utd|3utd]], [[3uv3|3uv3]], [[3uv7|3uv7]], [[3uv8|3uv8]], [[3uwm|3uwm]]</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=0CH:4-HYDROXYBUTYL+TRIHYDROGEN+DIPHOSPHATE'>0CH</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ispH, lytB, yaaE, b0029, JW0027 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=3uv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uv6 OCA], [https://pdbe.org/3uv6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uv6 RCSB], [https://www.ebi.ac.uk/pdbsum/3uv6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uv6 ProSAT]</span></td></tr>
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<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>
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<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=3uv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uv6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uv6 RCSB], [http://www.ebi.ac.uk/pdbsum/3uv6 PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The final step of the methylerythritol phosphate isoprenoid biosynthesis pathway is catalysed by the iron-sulphur enzyme IspH, producing the universal precursors of terpenes: isopentenyl diphosphate and dimethylallyl diphosphate. Here we report an unforeseen reaction discovered during the investigation of the interaction of IspH with acetylene inhibitors by X-ray crystallography, Mossbauer, and nuclear magnetic resonance spectroscopy. In addition to its role as a 2H(+)/2e(-) reductase, IspH can hydrate acetylenes to aldehydes and ketones via anti-Markovnikov/Markovnikov addition. The reactions only occur with the oxidised protein and proceed via eta(1)-O-enolate intermediates. One of these is characterized crystallographically and contains a C4 ligand oxygen bound to the unique, fourth iron in the 4Fe-4S cluster: this intermediate subsequently hydrolyzes to produce an aldehyde product. This unexpected side to IspH reactivity is of interest in the context of the mechanism of action of other acetylene hydratases, as well as in the design of antiinfectives targeting IspH.
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Discovery of acetylene hydratase activity of the iron-sulphur protein IspH.,Span I, Wang K, Wang W, Zhang Y, Bacher A, Eisenreich W, Li K, Schulz C, Oldfield E, Groll M Nat Commun. 2012 Sep 4;3:1042. doi: 10.1038/ncomms2052. PMID:22948824<ref>PMID:22948824</ref>
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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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==See Also==
==See Also==
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*[[4-hydroxy-3-methylbut-2-enyl diphosphate reductase|4-hydroxy-3-methylbut-2-enyl diphosphate reductase]]
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*[[4-hydroxy-3-methylbut-2-enyl diphosphate reductase 3D structures|4-hydroxy-3-methylbut-2-enyl diphosphate reductase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__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: Escherichia coli]]
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[[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: Groll, M]]
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[[Category: Groll M]]
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[[Category: Oldfield, E]]
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[[Category: Oldfield E]]
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[[Category: Schulz, C]]
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[[Category: Schulz C]]
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[[Category: Span, I]]
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[[Category: Span I]]
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[[Category: Wang, K]]
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[[Category: Wang K]]
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[[Category: Wang, W]]
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[[Category: Wang W]]
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[[Category: Zhang, Y]]
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[[Category: Zhang Y]]
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[[Category: Iron-sulfur protein]]
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[[Category: Isoprenoid biosynthesis]]
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[[Category: Isph]]
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[[Category: Lytb]]
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[[Category: Non-mevalonate pathway]]
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[[Category: Oxidoreductase]]
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Current revision

Ec_IspH in complex with 4-hydroxybutyl diphosphate (1301)

PDB ID 3uv6

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