3uv7: Difference between revisions

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[[Image:3uv7.jpg|left|200px]]


{{STRUCTURE_3uv7| PDB=3uv7 | SCENE= }}
==Ec_IspH in complex with buta-2,3-dienyl diphosphate (1300)==
<StructureSection load='3uv7' size='340' side='right'caption='[[3uv7]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3uv7]] 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=3UV7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UV7 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0CN:BUTA-2,3-DIEN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>0CN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></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=3uv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uv7 OCA], [https://pdbe.org/3uv7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uv7 RCSB], [https://www.ebi.ac.uk/pdbsum/3uv7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uv7 ProSAT]</span></td></tr>
</table>
== 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>


===Ec_IspH in complex with buta-2,3-dienyl diphosphate (1300)===
==See Also==
 
*[[4-hydroxy-3-methylbut-2-enyl diphosphate reductase 3D structures|4-hydroxy-3-methylbut-2-enyl diphosphate reductase 3D structures]]
 
== References ==
==About this Structure==
<references/>
[[3uv7]] 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=3UV7 OCA].
__TOC__
[[Category: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase]]
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli K-12]]
[[Category: Bacher, A.]]
[[Category: Large Structures]]
[[Category: Eisenreich, W.]]
[[Category: Bacher A]]
[[Category: Groll, M.]]
[[Category: Eisenreich W]]
[[Category: Oldfield, E.]]
[[Category: Groll M]]
[[Category: Schulz, C.]]
[[Category: Oldfield E]]
[[Category: Span, I.]]
[[Category: Schulz C]]
[[Category: Wang, K.]]
[[Category: Span I]]
[[Category: Wang, W.]]
[[Category: Wang K]]
[[Category: Zhang, Y.]]
[[Category: Wang W]]
[[Category: Iron-sulfur protein]]
[[Category: Zhang Y]]
[[Category: Isoprenoid biosynthesis]]
[[Category: Isph]]
[[Category: Lytb]]
[[Category: Non-mevalonate pathway]]
[[Category: Oxidoreductase]]

Latest revision as of 17:09, 14 March 2024

Ec_IspH in complex with buta-2,3-dienyl diphosphate (1300)Ec_IspH in complex with buta-2,3-dienyl diphosphate (1300)

Structural highlights

3uv7 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 1.6Å
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

3uv7, resolution 1.60Å

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