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1qb4

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

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Retrieved from "http://52.214.119.220/wiki/index.php/1qb4"

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-[[Image:1qb4.gif|left|200px]]<br /><applet load="1qb4" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1qb4, resolution 2.6&Aring;" />
-'''CRYSTAL STRUCTURE OF MN(2+)-BOUND PHOSPHOENOLPYRUVATE CARBOXYLASE'''<br />
-==Overview==
+==CRYSTAL STRUCTURE OF MN(2+)-BOUND PHOSPHOENOLPYRUVATE CARBOXYLASE==
-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.
+<StructureSection load='1qb4' size='340' side='right'caption='[[1qb4]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+<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>
+</table>
+== Function ==
+[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]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qb/1qb4_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-QB4 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 MN and ASP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QB4 OCA].
+*[[Phosphoenolpyruvate carboxylase|Phosphoenolpyruvate carboxylase]]
+__TOC__
-==Reference==
+</StructureSection>
-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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10481043 10481043]
 [[Category: Escherichia coli]]
-[[Category: Phosphoenolpyruvate carboxylase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Inoue T]]
-[[Category: Inoue, T.]]
+[[Category: Izui K]]
-[[Category: Izui, K.]]
+[[Category: Kai Y]]
-[[Category: Kai, Y.]]
+[[Category: Matsumura H]]
-[[Category: Matsumura, H.]]
+[[Category: Shirakata S]]
-[[Category: Shirakata, S.]]
+[[Category: Terada M]]
-[[Category: Terada, M.]]
+[[Category: Yoshinaga T]]
-[[Category: Yoshinaga, T.]]
-[[Category: ASP]]
-[[Category: MN]]
-[[Category: alpha beta barrel]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:32:57 2007''

1qb4

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

Structural highlights

Function

Evolutionary Conservation

See Also

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