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==STRUCTURE OF GCPE (IspG) FROM THERMUS THERMOPHILUS HB27== | |||
<StructureSection load='2y0f' size='340' side='right'caption='[[2y0f]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2y0f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y0F 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]] 2.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=2y0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y0f OCA], [https://pdbe.org/2y0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y0f RCSB], [https://www.ebi.ac.uk/pdbsum/2y0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y0f ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ISPG_THET2 ISPG_THET2] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Isoprenoids are biosynthesized via the mevalonate or the 2-C-methyl-d-erythritol-4-phosphate (MEP) pathways the latter being used by most pathogenic bacteria, some parasitic protozoa, plant plastids, but not by animals. We determined the X-ray structure of the homodimeric [4Fe-4S] cluster carrying E-1-hydroxy-2-methyl-but-2-enyl-4-diphosphate synthase (GcpE) of Thermus thermophilus which catalyzes the penultimate reaction of the MEP pathway and is therefore an attractive target for drug development. The [4Fe-4S] cluster ligated to three cysteines and one glutamate is encapsulated at the intersubunit interface. The substrate binding site lies in front of an (alphabeta)(8) barrel. The great [4Fe-4S] cluster-substrate distance implicates large-scale domain rearrangements during the reaction cycle. STRUCTURED SUMMARY: gcpEbinds to gcpE by x-ray crystallography (View interaction). | |||
Structure of the E-1-hydroxy-2-methyl-but-2-enyl-4-diphosphate synthase (GcpE) from Thermus thermophilus.,Rekittke I, Nonaka T, Wiesner J, Demmer U, Warkentin E, Jomaa H, Ermler U FEBS Lett. 2010 Dec 15. PMID:21167158<ref>PMID:21167158</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2y0f" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[IspG|IspG]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: Thermus thermophilus]] | </StructureSection> | ||
[[Category: Demmer | [[Category: Large Structures]] | ||
[[Category: Ermler | [[Category: Thermus thermophilus HB27]] | ||
[[Category: Jomaa | [[Category: Demmer U]] | ||
[[Category: Nonaka | [[Category: Ermler U]] | ||
[[Category: Rekittke | [[Category: Jomaa H]] | ||
[[Category: Warkentin | [[Category: Nonaka T]] | ||
[[Category: Wiesner | [[Category: Rekittke I]] | ||
[[Category: Warkentin E]] | |||
[[Category: Wiesner J]] | |||
Latest revision as of 11:06, 23 August 2023
STRUCTURE OF GCPE (IspG) FROM THERMUS THERMOPHILUS HB27STRUCTURE OF GCPE (IspG) FROM THERMUS THERMOPHILUS HB27
Structural highlights
FunctionPublication Abstract from PubMedIsoprenoids are biosynthesized via the mevalonate or the 2-C-methyl-d-erythritol-4-phosphate (MEP) pathways the latter being used by most pathogenic bacteria, some parasitic protozoa, plant plastids, but not by animals. We determined the X-ray structure of the homodimeric [4Fe-4S] cluster carrying E-1-hydroxy-2-methyl-but-2-enyl-4-diphosphate synthase (GcpE) of Thermus thermophilus which catalyzes the penultimate reaction of the MEP pathway and is therefore an attractive target for drug development. The [4Fe-4S] cluster ligated to three cysteines and one glutamate is encapsulated at the intersubunit interface. The substrate binding site lies in front of an (alphabeta)(8) barrel. The great [4Fe-4S] cluster-substrate distance implicates large-scale domain rearrangements during the reaction cycle. STRUCTURED SUMMARY: gcpEbinds to gcpE by x-ray crystallography (View interaction). Structure of the E-1-hydroxy-2-methyl-but-2-enyl-4-diphosphate synthase (GcpE) from Thermus thermophilus.,Rekittke I, Nonaka T, Wiesner J, Demmer U, Warkentin E, Jomaa H, Ermler U FEBS Lett. 2010 Dec 15. PMID:21167158[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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