View source for 3noy


==Crystal structure of IspG (gcpE)==
<StructureSection load='3noy' size='340' side='right'caption='[[3noy]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3noy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NOY 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]] 2.7&#8491;</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=3noy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3noy OCA], [https://pdbe.org/3noy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3noy RCSB], [https://www.ebi.ac.uk/pdbsum/3noy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3noy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ISPG_AQUAE ISPG_AQUAE] Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.<ref>PMID:20932974</ref> 
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== Publication Abstract from PubMed ==
IspG protein serves as the penultimate enzyme of the recently discovered non-mevalonate pathway for the biosynthesis of the universal isoprenoid precursors, isopentenyl diphosphate and dimethylallyl diphosphate. The enzyme catalyzes the reductive ring opening of 2C-methyl-d-erythritol 2,4-cyclodiphosphate, which affords 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. The protein was crystallized under anaerobic conditions, and its three-dimensional structure was determined to a resolution of 2.7 A. Each subunit of the c(2) symmetric homodimer folds into two domains connected by a short linker sequence. The N-terminal domain (N domain) is an eight-stranded beta barrel that belongs to the large TIM-barrel superfamily. The C-terminal domain (C domain) consists of a beta sheet that is flanked on both sides by helices. One glutamate and three cysteine residues of the C domain coordinate a [4Fe-4S] cluster. Homodimer formation involves an extended contact area (about 1100 A(2)) between helices 8 and 9 of each respective beta barrel. Moreover, each C domain contacts the N domain of the partner subunit, but the interface regions are small (about 430 A(2)). We propose that the enzyme substrate binds to the positively charged surface area at the C-terminal pole of the beta barrel. The C domain carrying the iron-sulfur cluster could then move over to form a closed conformation where the substrate is sandwiched between the N domain and the C domain. This article completes the set of three-dimensional structures of the non-mevalonate pathway enzymes, which are of specific interest as potential targets for tuberculostatic and antimalarial drugs.

Biosynthesis of Isoprenoids: Crystal Structure of the [4Fe-4S] Cluster Protein IspG.,Lee M, Grawert T, Quitterer F, Rohdich F, Eppinger J, Eisenreich W, Bacher A, Groll M J Mol Biol. 2010 Oct 7. PMID:20932974<ref>PMID:20932974</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3noy" style="background-color:#fffaf0;"></div>

==See Also==
*[[IspG|IspG]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aquifex aeolicus]]
[[Category: Large Structures]]
[[Category: Bacher A]]
[[Category: Graewert T]]
[[Category: Groll M]]