1i9a

<StructureSection load='1i9a' size='340' side='right'caption='[[1i9a]], [[Resolution|resolution]] 2.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[1i9a]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I9A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I9A FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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=1i9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9a OCA], [http://pdbe.org/1i9a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i9a RCSB], [http://www.ebi.ac.uk/pdbsum/1i9a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1i9a ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/1i9a TOPSAN]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/IDI_ECOLI IDI_ECOLI]] Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).<ref>PMID:10099534</ref> <ref>PMID:9603997</ref>

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== Publication Abstract from PubMed ==

X-ray structures of two enzymes in the sterol/isoprenoid biosynthesis pathway have been determined in a structural genomics pilot study. Mevalonate-5-diphosphate decarboxylase (MDD) is a single-domain alpha/beta protein that catalyzes the last of three sequential ATP-dependent reactions which convert mevalonate to isopentenyl diphosphate. Isopentenyl disphosphate isomerase (IDI) is an alpha/beta metalloenzyme that catalyzes interconversion of isopentenyl diphosphate and dimethylallyl diphosphate, which condense in the next step toward synthesis of sterols and a host of natural products. Homology modeling of related proteins and comparisons of the MDD and IDI structures with two other experimentally determined structures have shown that MDD is a member of the GHMP superfamily of small-molecule kinases and IDI is similar to the nudix hydrolases, which act on nucleotide diphosphatecontaining substrates. Structural models were produced for 379 proteins, encompassing a substantial fraction of both protein superfamilies. All three enzymes responsible for synthesis of isopentenyl diphosphate from mevalonate (mevalonate kinase, phosphomevalonate kinase, and MDD) share the same fold, catalyze phosphorylation of chemically similar substrates (MDD decarboxylation involves phosphorylation of mevalonate diphosphate), and seem to have evolved from a common ancestor. These structures and the structural models derived from them provide a framework for interpreting biochemical function and evolutionary relationships.

Structural genomics of enzymes involved in sterol/isoprenoid biosynthesis.,Bonanno JB, Edo C, Eswar N, Pieper U, Romanowski MJ, Ilyin V, Gerchman SE, Kycia H, Studier FW, Sali A, Burley SK Proc Natl Acad Sci U S A. 2001 Nov 6;98(23):12896-901. PMID:11698677<ref>PMID:11698677</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 1i9a" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Isopentenyl-diphosphate Delta-isomerase]]

[[Category: Bonanno, J B]]

[[Category: Burley, S K]]

[[Category: Edo, C]]

[[Category: Eswar, N]]

[[Category: Gerchman, S E]]

[[Category: Ilyin, V]]

[[Category: Kycia, H]]

[[Category: Structural genomic]]

[[Category: Pieper, U]]

[[Category: Romanowski, M J]]

[[Category: Sali, A]]

[[Category: Studier, F W]]

[[Category: PSI, Protein structure initiative]]