2g73

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{{Seed}}
 
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[[Image:2g73.png|left|200px]]
 
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==Y104F mutant type 1 IPP isomerase complex with EIPP==
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The line below this paragraph, containing "STRUCTURE_2g73", creates the "Structure Box" on the page.
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<StructureSection load='2g73' size='340' side='right'caption='[[2g73]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2g73]] 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=2G73 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G73 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]] 1.97&#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=EIP:4-HYDROXY-3-METHYL+BUTYL+DIPHOSPHATE'>EIP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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{{STRUCTURE_2g73| PDB=2g73 | SCENE= }}
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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=2g73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g73 OCA], [https://pdbe.org/2g73 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g73 RCSB], [https://www.ebi.ac.uk/pdbsum/2g73 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g73 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/g7/2g73_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=2g73 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Isopentenyl-diphosphate (IPP):dimethylallyl diphosphate isomerase is a key enzyme in the biosynthesis of isoprenoids. The mechanism of the isomerization reaction involves protonation of the unactivated carbon-carbon double bond in the substrate, but identity of the acidic moiety providing the proton is still not clear. Multiple sequence alignments and geometrical features observed in crystal structures of complexes with IPP isomerase suggest that Tyr-104 could play an important role during catalysis. A series of mutants was constructed by directed mutagenesis and characterized by enzymology. Crystallographic and thermal denaturation data for Y104A and Y104F mutants were obtained. Those data demonstrate the importance of residue Tyr-104 for proper folding of Escherichia coli type I IPP isomerase.
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===Y104F mutant type 1 IPP isomerase complex with EIPP===
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Structural role for Tyr-104 in Escherichia coli isopentenyl-diphosphate isomerase: site-directed mutagenesis, enzymology, and protein crystallography.,de Ruyck J, Durisotti V, Oudjama Y, Wouters J J Biol Chem. 2006 Jun 30;281(26):17864-9. Epub 2006 Apr 15. PMID:16617181<ref>PMID:16617181</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2g73" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_16617181}}, adds the Publication Abstract to the page
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*[[Isopentenyl-diphosphate delta-isomerase|Isopentenyl-diphosphate delta-isomerase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 16617181 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16617181}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2G73 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G73 OCA].
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==Reference==
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Structural role for Tyr-104 in Escherichia coli isopentenyl-diphosphate isomerase: site-directed mutagenesis, enzymology, and protein crystallography., de Ruyck J, Durisotti V, Oudjama Y, Wouters J, J Biol Chem. 2006 Jun 30;281(26):17864-9. Epub 2006 Apr 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16617181 16617181]
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[[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: Pdbx_ordinal=, <PDBx:audit_author.]]
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[[Category: Wouters J]]
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[[Category: Complex]]
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[[Category: De Ruyck J]]
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[[Category: Isomerase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Dec 5 09:44:58 2008''
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Current revision

Y104F mutant type 1 IPP isomerase complex with EIPP

PDB ID 2g73

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