4h4c: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "4h4c" [edit=sysop:move=sysop] |
No edit summary |
||
| (8 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==IspH in complex with (E)-4-fluoro-3-methylbut-2-enyl diphosphate== | |||
<StructureSection load='4h4c' size='340' side='right'caption='[[4h4c]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4h4c]] 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=4H4C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H4C 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]] 1.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=10D:(2E)-4-FLUORO-3-METHYLBUT-2-EN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>10D</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=4h4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h4c OCA], [https://pdbe.org/4h4c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h4c RCSB], [https://www.ebi.ac.uk/pdbsum/4h4c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h4c 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> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4h4c" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[4-hydroxy-3-methylbut-2-enyl diphosphate reductase 3D structures|4-hydroxy-3-methylbut-2-enyl diphosphate reductase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Bacher A]] | |||
[[Category: Eisenreich W]] | |||
[[Category: Groll M]] | |||
[[Category: Jauch J]] | |||
[[Category: Span I]] | |||
Latest revision as of 11:04, 13 August 2026
IspH in complex with (E)-4-fluoro-3-methylbut-2-enyl diphosphate
| ||||||||||||
