1hzt

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(New page: 200px<br /><applet load="1hzt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hzt, resolution 1.45&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1hzt.jpg|left|200px]]<br /><applet load="1hzt" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hzt, resolution 1.45&Aring;" />
 
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'''CRYSTAL STRUCTURE OF METAL-FREE ISOPENTENYL DIPHOSPHATE:DIMETHYLALLYL DIPHOSPHATE ISOMERASE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF METAL-FREE ISOPENTENYL DIPHOSPHATE:DIMETHYLALLYL DIPHOSPHATE ISOMERASE==
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Isopentenyl diphosphate:dimethylallyl diphosphate (IPP:DMAPP) isomerase, catalyses a crucial activation step in the isoprenoid biosynthesis, pathway. This enzyme is responsible for the isomerization of the, carbon-carbon double bond of IPP to create the potent electrophile DMAPP., DMAPP then alkylates other molecules, including IPP, to initiate the, extraordinary variety of isoprenoid compounds found in nature. The crystal, structures of free and metal-bound Escherichia coli IPP isomerase reveal, critical active site features underlying its catalytic mechanism. The, enzyme requires one Mn(2+) or Mg(2+) ion to fold in its active, conformation, forming a distorted octahedral metal coordination site, composed of three histidines and two glutamates and located in the active, site. Two critical residues, C67 and E116, face each other within the, active site, close to the metal-binding site. The structures are, compatible with a mechanism in which the cysteine initiates the reaction, by protonating the carbon-carbon double bond, with the antarafacial, rearrangement ultimately achieved by one of the glutamates involved in the, metal coordination sphere. W161 may stabilize the highly reactive, carbocation generated during the reaction through quadrupole- charge, interaction.
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<StructureSection load='1hzt' size='340' side='right'caption='[[1hzt]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1hzt]] is a 1 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=1HZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HZT FirstGlance]. <br>
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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]] 1.45&#8491;</td></tr>
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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=1hzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hzt OCA], [https://pdbe.org/1hzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hzt RCSB], [https://www.ebi.ac.uk/pdbsum/1hzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hzt ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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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/hz/1hzt_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=1hzt ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1HZT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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=1HZT OCA].
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*[[Isopentenyl-diphosphate delta-isomerase|Isopentenyl-diphosphate delta-isomerase]]
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== References ==
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==Reference==
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<references/>
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Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase., Durbecq V, Sainz G, Oudjama Y, Clantin B, Bompard-Gilles C, Tricot C, Caillet J, Stalon V, Droogmans L, Villeret V, EMBO J. 2001 Apr 2;20(7):1530-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11285217 11285217]
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Isopentenyl-diphosphate Delta-isomerase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Bompard-Gilles C]]
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[[Category: Bompard-Gilles, C.]]
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[[Category: Caillet J]]
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[[Category: Caillet, J.]]
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[[Category: Clantin B]]
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[[Category: Clantin, B.]]
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[[Category: Droogmans L]]
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[[Category: Droogmans, L.]]
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[[Category: Durbecq V]]
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[[Category: Durbecq, V.]]
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[[Category: Oudjama Y]]
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[[Category: Oudjama, Y.]]
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[[Category: Sainz G]]
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[[Category: Sainz, G.]]
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[[Category: Stalon V]]
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[[Category: Stalon, V.]]
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[[Category: Tricot C]]
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[[Category: Tricot, C.]]
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[[Category: Villeret V]]
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[[Category: Villeret, V.]]
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[[Category: dimethylallyl]]
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[[Category: isomerase]]
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[[Category: isopentenyl]]
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[[Category: isoprenoids]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:56:17 2007''
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Current revision

CRYSTAL STRUCTURE OF METAL-FREE ISOPENTENYL DIPHOSPHATE:DIMETHYLALLYL DIPHOSPHATE ISOMERASE

PDB ID 1hzt

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