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1fiy

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[[Image:1fiy.gif|left|200px]]
 
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{{Structure
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==THREE-DIMENSIONAL STRUCTURE OF PHOSPHOENOLPYRUVATE CARBOXYLASE FROM ESCHERICHIA COLI AT 2.8 A RESOLUTION==
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|PDB= 1fiy |SIZE=350|CAPTION= <scene name='initialview01'>1fiy</scene>, resolution 2.8&Aring;
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<StructureSection load='1fiy' size='340' side='right'caption='[[1fiy]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ASP:ASPARTIC ACID'>ASP</scene>
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<table><tr><td colspan='2'>[[1fiy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FIY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FIY 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]] 2.8&#8491;</td></tr>
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|GENE=
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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></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=1fiy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fiy OCA], [https://pdbe.org/1fiy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fiy RCSB], [https://www.ebi.ac.uk/pdbsum/1fiy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fiy 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/fi/1fiy_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=1fiy ConSurf].
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<div style="clear:both"></div>
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'''THREE-DIMENSIONAL STRUCTURE OF PHOSPHOENOLPYRUVATE CARBOXYLASE FROM ESCHERICHIA COLI AT 2.8 A RESOLUTION'''
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==See Also==
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*[[Phosphoenolpyruvate carboxykinase 3D structures|Phosphoenolpyruvate carboxykinase 3D structures]]
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*[[Phosphoenolpyruvate carboxylase|Phosphoenolpyruvate carboxylase]]
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==Overview==
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__TOC__
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The crystal structure of phosphoenolpyruvate carboxylase (PEPC; EC 4. 1.1.31) has been determined by x-ray diffraction methods at 2.8-A resolution by using Escherichia coli PEPC complexed with L-aspartate, an allosteric inhibitor of all known PEPCs. The four subunits are arranged in a "dimer-of-dimers" form with respect to subunit contact, resulting in an overall square arrangement. The contents of alpha-helices and beta-strands are 65% and 5%, respectively. All of the eight beta-strands, which are widely dispersed in the primary structure, participate in the formation of a single beta-barrel. Replacement of a conserved Arg residue (Arg-438) in this linkage with Cys increased the tendency of the enzyme to dissociate into dimers. The location of the catalytic site is likely to be near the C-terminal side of the beta-barrel. The binding site for L-aspartate is located about 20 A away from the catalytic site, and four residues (Lys-773, Arg-832, Arg-587, and Asn-881) are involved in effector binding. The participation of Arg-587 is unexpected, because it is known to be catalytically essential. Because this residue is in a highly conserved glycine-rich loop, which is characteristic of PEPC, L-aspartate seemingly causes inhibition by removing this glycine-rich loop from the catalytic site. There is another mobile loop from Lys-702 to Gly-708 that is missing in the crystal structure. The importance of this loop in catalytic activity was also shown. Thus, the crystal-structure determination of PEPC revealed two mobile loops bearing the enzymatic functions and accompanying allosteric inhibition by L-aspartate.
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</StructureSection>
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[[Category: Escherichia coli K-12]]
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==About this Structure==
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[[Category: Large Structures]]
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1FIY 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=1FIY OCA].
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[[Category: Inoue T]]
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[[Category: Izui K]]
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==Reference==
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[[Category: Kai Y]]
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Three-dimensional structure of phosphoenolpyruvate carboxylase: a proposed mechanism for allosteric inhibition., Kai Y, Matsumura H, Inoue T, Terada K, Nagara Y, Yoshinaga T, Kihara A, Tsumura K, Izui K, Proc Natl Acad Sci U S A. 1999 Feb 2;96(3):823-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9927652 9927652]
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[[Category: Kihara A]]
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[[Category: Escherichia coli]]
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[[Category: Matsumura H]]
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[[Category: Phosphoenolpyruvate carboxylase]]
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[[Category: Nagara Y]]
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[[Category: Single protein]]
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[[Category: Terada K]]
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[[Category: Inoue, T.]]
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[[Category: Yoshinaga T]]
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[[Category: Izui, K.]]
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[[Category: Kai, Y.]]
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[[Category: Kihara, A.]]
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[[Category: Matsumura, H.]]
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[[Category: Nagara, Y.]]
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[[Category: Terada, K.]]
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[[Category: Yoshinaga, T.]]
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[[Category: ASP]]
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[[Category: carboxylase]]
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[[Category: complex (lyase/inhibitor)]]
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[[Category: phosphoenolpyruvate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:09:41 2008''
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Current revision

THREE-DIMENSIONAL STRUCTURE OF PHOSPHOENOLPYRUVATE CARBOXYLASE FROM ESCHERICHIA COLI AT 2.8 A RESOLUTION

PDB ID 1fiy

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