1igw

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(New page: 200px<br /><applet load="1igw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1igw, resolution 2.1&Aring;" /> '''Crystal Structure of ...)
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[[Image:1igw.gif|left|200px]]<br /><applet load="1igw" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1igw, resolution 2.1&Aring;" />
 
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'''Crystal Structure of the Isocitrate Lyase from the A219C mutant of Escherichia coli'''<br />
 
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==Overview==
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==Crystal Structure of the Isocitrate Lyase from the A219C mutant of Escherichia coli==
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Enzymes of the glyoxylate-bypass pathway are potential targets for the, control of many human diseases caused by such pathogens as Mycobacteria, and Leishmania. Isocitrate lyase catalyses the first committed step in, this pathway and the structure of this tetrameric enzyme from Escherichia, coli has been determined at 2.1 A resolution. E. coli isocitrate lyase, like the enzyme from other prokaryotes, is located in the cytoplasm, whereas in plants, protozoa, algae and fungi this enzyme is found, localized in glyoxysomes. Comparison of the structure of the prokaryotic, isocitrate lyase with that from the eukaryote Aspergillus nidulans reveals, a different domain structure following the deletion of approximately 100, residues from the larger eukaryotic enzyme. Despite this, the active sites, of the prokaryotic and eukaryotic enzymes are very closely related, including the apparent disorder of two equivalent segments of the protein, that are known to be involved in a conformational change as part of the, enzyme's catalytic cycle.
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<StructureSection load='1igw' size='340' side='right'caption='[[1igw]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1igw]] is a 4 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=1IGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IGW 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]] 2.1&#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=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></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=1igw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1igw OCA], [https://pdbe.org/1igw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1igw RCSB], [https://www.ebi.ac.uk/pdbsum/1igw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1igw ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ACEA_ECOLI ACEA_ECOLI] Catalyzes the formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle. May be involved in the assimilation of one-carbon compounds via the isocitrate lyase-positive serine pathway (By similarity).
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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/ig/1igw_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=1igw 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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Enzymes of the glyoxylate-bypass pathway are potential targets for the control of many human diseases caused by such pathogens as Mycobacteria and Leishmania. Isocitrate lyase catalyses the first committed step in this pathway and the structure of this tetrameric enzyme from Escherichia coli has been determined at 2.1 A resolution. E. coli isocitrate lyase, like the enzyme from other prokaryotes, is located in the cytoplasm, whereas in plants, protozoa, algae and fungi this enzyme is found localized in glyoxysomes. Comparison of the structure of the prokaryotic isocitrate lyase with that from the eukaryote Aspergillus nidulans reveals a different domain structure following the deletion of approximately 100 residues from the larger eukaryotic enzyme. Despite this, the active sites of the prokaryotic and eukaryotic enzymes are very closely related, including the apparent disorder of two equivalent segments of the protein that are known to be involved in a conformational change as part of the enzyme's catalytic cycle.
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==About this Structure==
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The structure and domain organization of Escherichia coli isocitrate lyase.,Britton KL, Abeysinghe IS, Baker PJ, Barynin V, Diehl P, Langridge SJ, McFadden BA, Sedelnikova SE, Stillman TJ, Weeradechapon K, Rice DW Acta Crystallogr D Biol Crystallogr. 2001 Sep;57(Pt 9):1209-18. Epub 2001, Aug 23. PMID:11526312<ref>PMID:11526312</ref>
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1IGW 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 HG, MG and PYR as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Isocitrate_lyase Isocitrate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.1 4.1.3.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IGW OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The structure and domain organization of Escherichia coli isocitrate lyase., Britton KL, Abeysinghe IS, Baker PJ, Barynin V, Diehl P, Langridge SJ, McFadden BA, Sedelnikova SE, Stillman TJ, Weeradechapon K, Rice DW, Acta Crystallogr D Biol Crystallogr. 2001 Sep;57(Pt 9):1209-18. Epub 2001, Aug 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11526312 11526312]
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</div>
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<div class="pdbe-citations 1igw" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Isocitrate lyase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Abeysinghe ISB]]
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[[Category: Abeysinghe, I.S.B.]]
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[[Category: Baker PJ]]
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[[Category: Baker, P.J.]]
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[[Category: Barynin V]]
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[[Category: Barynin, V.]]
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[[Category: Britton KL]]
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[[Category: Britton, K.L.]]
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[[Category: Diehl P]]
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[[Category: Diehl, P.]]
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[[Category: Langridge SJ]]
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[[Category: Langridge, S.J.]]
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[[Category: McFadden BA]]
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[[Category: McFadden, B.A.]]
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[[Category: Rice DW]]
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[[Category: Rice, D.W.]]
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[[Category: Sedelnikova SE]]
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[[Category: Sedelnikova, S.E.]]
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[[Category: Stillman TJ]]
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[[Category: Stillman, T.J.]]
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[[Category: Weeradechapon K]]
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[[Category: Weeradechapon, K.]]
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[[Category: HG]]
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[[Category: MG]]
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[[Category: PYR]]
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[[Category: beta barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:23:26 2007''
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Current revision

Crystal Structure of the Isocitrate Lyase from the A219C mutant of Escherichia coli

PDB ID 1igw

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