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1fi4

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(New page: 200px<br /><applet load="1fi4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fi4, resolution 2.27&Aring;" /> '''THE X-RAY CRYSTAL ST...)
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[[Image:1fi4.gif|left|200px]]<br /><applet load="1fi4" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fi4, resolution 2.27&Aring;" />
 
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'''THE X-RAY CRYSTAL STRUCTURE OF MEVALONATE 5-DIPHOSPHATE DECARBOXYLASE AT 2.3 ANGSTROM RESOLUTION.'''<br />
 
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==Overview==
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==THE X-RAY CRYSTAL STRUCTURE OF MEVALONATE 5-DIPHOSPHATE DECARBOXYLASE AT 2.3 ANGSTROM RESOLUTION.==
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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.
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<StructureSection load='1fi4' size='340' side='right'caption='[[1fi4]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1fi4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FI4 FirstGlance]. <br>
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1FI4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/Diphosphomevalonate_decarboxylase Diphosphomevalonate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.33 4.1.1.33] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FI4 OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.27&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fi4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fi4 OCA], [https://pdbe.org/1fi4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fi4 RCSB], [https://www.ebi.ac.uk/pdbsum/1fi4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fi4 ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1fi4 TOPSAN]</span></td></tr>
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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]
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</table>
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[[Category: Diphosphomevalonate decarboxylase]]
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== Function ==
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[https://www.uniprot.org/uniprot/MVD1_YEAST MVD1_YEAST]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fi/1fi4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1fi4 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Bonanno JB]]
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[[Category: Bonanno, J.B.]]
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[[Category: Burley SK]]
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[[Category: Burley, S.K.]]
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[[Category: Edo C]]
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[[Category: Edo, C.]]
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[[Category: Eswar N]]
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[[Category: Eswar, N.]]
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[[Category: Gerchman SE]]
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[[Category: Gerchman, S.E.]]
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[[Category: Ilyin V]]
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[[Category: Ilyin, V.]]
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[[Category: Kycia H]]
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[[Category: Kycia, H.]]
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[[Category: Pieper U]]
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[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
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[[Category: Romanowski MJ]]
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[[Category: Pieper, U.]]
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[[Category: Sali A]]
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[[Category: Romanowski, M.J.]]
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[[Category: Studier FW]]
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[[Category: Sali, A.]]
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[[Category: Studier, F.W.]]
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[[Category: atp binding]]
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[[Category: cholesterol biosynthesis]]
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[[Category: decarboxylase]]
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[[Category: mixed alpha/beta structure]]
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[[Category: new york structural genomix research consortium]]
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[[Category: nysgxrc]]
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[[Category: protein structure initiative]]
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[[Category: psi]]
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[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:56:27 2007''
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Current revision

THE X-RAY CRYSTAL STRUCTURE OF MEVALONATE 5-DIPHOSPHATE DECARBOXYLASE AT 2.3 ANGSTROM RESOLUTION.

PDB ID 1fi4

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