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<StructureSection load='3utc' size='340' side='right'caption='[[3utc]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3utc' size='340' side='right'caption='[[3utc]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3utc]] 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=3UTC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UTC FirstGlance]. <br>
<table><tr><td colspan='2'>[[3utc]] 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=3UTC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UTC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0JX:(3E)-4-HYDROXYBUT-3-EN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>0JX</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ke8|3ke8]], [[3dnf|3dnf]], [[3urk|3urk]], [[3utd|3utd]], [[3uv3|3uv3]], [[3uv6|3uv6]], [[3uv7|3uv7]], [[3uv8|3uv8]], [[3uwm|3uwm]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0JX:(3E)-4-HYDROXYBUT-3-EN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>0JX</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ispH, lytB, yaaE, b0029, JW0027 ([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'>[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'>[https://proteopedia.org/fgij/fg.htm?mol=3utc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3utc OCA], [https://pdbe.org/3utc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3utc RCSB], [https://www.ebi.ac.uk/pdbsum/3utc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3utc 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=3utc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3utc OCA], [https://pdbe.org/3utc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3utc RCSB], [https://www.ebi.ac.uk/pdbsum/3utc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3utc 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> 
[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>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3utc" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]]
[[Category: Escherichia coli K-12]]
[[Category: Ecoli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bacher, A]]
[[Category: Bacher A]]
[[Category: Eisenreich, W]]
[[Category: Eisenreich W]]
[[Category: Groll, M]]
[[Category: Groll M]]
[[Category: Li, K]]
[[Category: Li K]]
[[Category: Oldfield, E]]
[[Category: Oldfield E]]
[[Category: Schulz, C]]
[[Category: Schulz C]]
[[Category: Span, I]]
[[Category: Span I]]
[[Category: Wang, K]]
[[Category: Wang K]]
[[Category: Wang, W]]
[[Category: Wang W]]
[[Category: Zhang, Y]]
[[Category: Zhang Y]]
[[Category: Iron-sulfur protein]]
[[Category: Isoprenoid biosynthesis]]
[[Category: Isph]]
[[Category: Lytb]]
[[Category: Non-mevalonate pathway]]
[[Category: Oxidoreductase]]

Revision as of 14:07, 14 March 2024

Ec_IspH in complex with (E)-4-hydroxybut-3-enyl diphosphate

3utc, resolution 1.90Å

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