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1qb4

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[[Image:1qb4.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF MN(2+)-BOUND PHOSPHOENOLPYRUVATE CARBOXYLASE==
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|PDB= 1qb4 |SIZE=350|CAPTION= <scene name='initialview01'>1qb4</scene>, resolution 2.6&Aring;
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<StructureSection load='1qb4' size='340' side='right'caption='[[1qb4]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=ASP:ASPARTIC ACID'>ASP</scene>
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<table><tr><td colspan='2'>[[1qb4]] 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=1QB4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QB4 FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxylase Phosphoenolpyruvate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.31 4.1.1.31]
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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]] 2.6&#8491;</td></tr>
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|GENE= K12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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}}
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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=1qb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qb4 OCA], [https://pdbe.org/1qb4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qb4 RCSB], [https://www.ebi.ac.uk/pdbsum/1qb4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qb4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAPP_ECOLI CAPP_ECOLI] Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.[HAMAP-Rule:MF_00595]
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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/qb/1qb4_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=1qb4 ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF MN(2+)-BOUND PHOSPHOENOLPYRUVATE CARBOXYLASE'''
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==See Also==
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*[[Phosphoenolpyruvate carboxylase|Phosphoenolpyruvate carboxylase]]
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__TOC__
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==Overview==
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</StructureSection>
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We have determined the crystal structure of Mn2+-bound Escherichia coli phosphoenolpyruvate carboxylase (PEPC) using X-ray diffraction at 2.6 A resolution, and specified the location of enzyme-bound Mn2+, which is essential for catalytic activity. The electron density map reveals that Mn2+ is bound to the side chain oxygens of Glu-506 and Asp-543, and located at the top of the alpha/beta barrel in PEPC. The coordination sphere of Mn2+ observed in E. coli PEPC is similar to that of Mn2+ found in the pyruvate kinase structure. The model study of Mn2+-bound PEPC complexed with phosphoenolpyruvate (PEP) reveals that the side chains of Arg-396, Arg-581 and Arg-713 could interact with PEP.
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==About this Structure==
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1QB4 is a [[Single protein]] structure of sequence 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=1QB4 OCA].
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==Reference==
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Plausible phosphoenolpyruvate binding site revealed by 2.6 A structure of Mn2+-bound phosphoenolpyruvate carboxylase from Escherichia coli., Matsumura H, Terada M, Shirakata S, Inoue T, Yoshinaga T, Izui K, Kai Y, FEBS Lett. 1999 Sep 17;458(2):93-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10481043 10481043]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Phosphoenolpyruvate carboxylase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Inoue T]]
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[[Category: Inoue, T.]]
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[[Category: Izui K]]
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[[Category: Izui, K.]]
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[[Category: Kai Y]]
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[[Category: Kai, Y.]]
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[[Category: Matsumura H]]
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[[Category: Matsumura, H.]]
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[[Category: Shirakata S]]
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[[Category: Shirakata, S.]]
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[[Category: Terada M]]
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[[Category: Terada, M.]]
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[[Category: Yoshinaga T]]
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[[Category: Yoshinaga, T.]]
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[[Category: ASP]]
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[[Category: MN]]
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[[Category: alpha beta barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:35:19 2008''
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Current revision

CRYSTAL STRUCTURE OF MN(2+)-BOUND PHOSPHOENOLPYRUVATE CARBOXYLASE

PDB ID 1qb4

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