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1i9a

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STRUCTURAL STUDIES OF CHOLESTEROL BIOSYNTHESIS: MEVALONATE 5-DIPHOSPHATE DECARBOXYLASE AND ISOPENTENYL DIPHOSPHATE ISOMERASE

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Retrieved from "http://52.214.119.220/wiki/index.php/1i9a"

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-[[Image:1i9a.gif|left|200px]]<br /><applet load="1i9a" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1i9a, resolution 2.5&Aring;" />
-'''STRUCTURAL STUDIES OF CHOLESTEROL BIOSYNTHESIS: MEVALONATE 5-DIPHOSPHATE DECARBOXYLASE AND ISOPENTENYL DIPHOSPHATE ISOMERASE'''<br />
-==Overview==
+==STRUCTURAL STUDIES OF CHOLESTEROL BIOSYNTHESIS: MEVALONATE 5-DIPHOSPHATE DECARBOXYLASE AND ISOPENTENYL DIPHOSPHATE ISOMERASE==
-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.
+<StructureSection load='1i9a' size='340' side='right'caption='[[1i9a]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1i9a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1I9A 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]] 2.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1i9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9a OCA], [https://pdbe.org/1i9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i9a RCSB], [https://www.ebi.ac.uk/pdbsum/1i9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i9a ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1i9a TOPSAN]</span></td></tr>
+</table>
+== Function ==
+[https://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>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i9/1i9a_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1i9a ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-I9A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Isopentenyl-diphosphate_Delta-isomerase Isopentenyl-diphosphate Delta-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.2 5.3.3.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I9A OCA].
+*[[Isopentenyl-diphosphate delta-isomerase|Isopentenyl-diphosphate delta-isomerase]]
+== References ==
-==Reference==
+<references/>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11698677 11698677]
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Isopentenyl-diphosphate Delta-isomerase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Bonanno JB]]
-[[Category: Bonanno, J.B.]]
+[[Category: Burley SK]]
-[[Category: Burley, S.K.]]
+[[Category: Edo C]]
-[[Category: Edo, C.]]
+[[Category: Eswar N]]
-[[Category: Eswar, N.]]
+[[Category: Gerchman SE]]
-[[Category: Gerchman, S.E.]]
+[[Category: Ilyin V]]
-[[Category: Ilyin, V.]]
+[[Category: Kycia H]]
-[[Category: Kycia, H.]]
+[[Category: Pieper U]]
-[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
+[[Category: Romanowski MJ]]
-[[Category: Pieper, U.]]
+[[Category: Sali A]]
-[[Category: Romanowski, M.J.]]
+[[Category: Studier FW]]
-[[Category: Sali, A.]]
-[[Category: Studier, F.W.]]
-[[Category: MN]]
-[[Category: alpha/beta protein]]
-[[Category: isomerase]]
-[[Category: mn2+]]
-[[Category: new york structural genomix research consortium]]
-[[Category: nysgxrc]]
-[[Category: protein structure initiative]]
-[[Category: psi]]
-[[Category: structural genomics]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:11:36 2007''

1i9a

From Proteopedia

Current revision

STRUCTURAL STUDIES OF CHOLESTEROL BIOSYNTHESIS: MEVALONATE 5-DIPHOSPHATE DECARBOXYLASE AND ISOPENTENYL DIPHOSPHATE ISOMERASE

Structural highlights

Function

Evolutionary Conservation

See Also

References

Contents

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