3utd: Difference between revisions

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==Ec_IspH in complex with 4-oxopentyl diphosphate==
==Ec_IspH in complex with 4-oxopentyl diphosphate==
<StructureSection load='3utd' size='340' side='right' caption='[[3utd]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='3utd' size='340' side='right'caption='[[3utd]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3utd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UTD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UTD FirstGlance]. <br>
<table><tr><td colspan='2'>[[3utd]] 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=3UTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UTD FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0CJ:4-OXOPENTYL+TRIHYDROGEN+DIPHOSPHATE'>0CJ</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</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]] 1.7&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ke8|3ke8]], [[3dnf|3dnf]], [[3urk|3urk]], [[3utc|3utc]], [[3uv3|3uv3]], [[3uv6|3uv6]], [[3uv7|3uv7]], [[3uv8|3uv8]], [[3uwm|3uwm]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0CJ:4-OXOPENTYL+TRIHYDROGEN+DIPHOSPHATE'>0CJ</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene></td></tr>
<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=83333 ECOLI])</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=3utd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3utd OCA], [https://pdbe.org/3utd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3utd RCSB], [https://www.ebi.ac.uk/pdbsum/3utd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3utd ProSAT]</span></td></tr>
<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>
<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=3utd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3utd OCA], [http://pdbe.org/3utd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3utd RCSB], [http://www.ebi.ac.uk/pdbsum/3utd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3utd ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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> 
[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 3utd" style="background-color:#fffaf0;"></div>


==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/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]]
[[Category: Escherichia coli K-12]]
[[Category: Ecoli]]
[[Category: Large Structures]]
[[Category: Bacher, A]]
[[Category: Bacher A]]
[[Category: Eisenreich, W]]
[[Category: Eisenreich W]]
[[Category: Groll, M]]
[[Category: Groll M]]
[[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]]

Latest revision as of 17:08, 14 March 2024

Ec_IspH in complex with 4-oxopentyl diphosphateEc_IspH in complex with 4-oxopentyl diphosphate

Structural highlights

3utd is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] [3]

See Also

References

  1. ↑ Grawert T, Rohdich F, Span I, Bacher A, Eisenreich W, Eppinger J, Groll M. Structure of active IspH enzyme from Escherichia coli provides mechanistic insights into substrate reduction. Angew Chem Int Ed Engl. 2009;48(31):5756-9. PMID:19569147 doi:10.1002/anie.200900548
  2. ↑ Grawert T, Span I, Eisenreich W, Rohdich F, Eppinger J, Bacher A, Groll M. Probing the reaction mechanism of IspH protein by x-ray structure analysis. Proc Natl Acad Sci U S A. 2010 Jan 19;107(3):1077-81. Epub 2009 Dec 28. PMID:20080550
  3. ↑ Span I, Grawert T, Bacher A, Eisenreich W, Groll M. Crystal Structures of Mutant IspH Proteins Reveal a Rotation of the Substrate's Hydroxymethyl Group during Catalysis. J Mol Biol. 2011 Nov 23. PMID:22137895 doi:10.1016/j.jmb.2011.11.033

3utd, resolution 1.70Å

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