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4c3t

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Revision as of 17:24, 7 September 2022

The Carbonic anhydrase from Thermovibrio ammonificans reveals an interesting intermolecular disulfide contributing to increasing thermal stability of this enzyme

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Retrieved from "http://52.214.119.220/wiki/index.php/4c3t"

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 <StructureSection load='4c3t' size='340' side='right'caption='[[4c3t]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4c3t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermovibrio_ammonificans Thermovibrio ammonificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C3T FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4c3t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermovibrio_ammonificans Thermovibrio ammonificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C3T FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </span></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=4c3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3t OCA], [https://pdbe.org/4c3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c3t RCSB], [https://www.ebi.ac.uk/pdbsum/4c3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c3t ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4c3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3t OCA], [http://pdbe.org/4c3t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c3t RCSB], [http://www.ebi.ac.uk/pdbsum/4c3t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c3t ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[[https://www.uniprot.org/uniprot/E8T502_THEA1 E8T502_THEA1]]
-Carbonic anhydrase enzymes catalyse the reversible hydration of carbon dioxide to bicarbonate. A thermophilic Thermovibrio ammonificans alpha-carbonic anhydrase (TaCA) has been expressed in Escherichia coli and structurally and biochemically characterized. The crystal structure of TaCA has been determined in its native form and in two complexes with bound inhibitors. The tetrameric enzyme is stabilized by a unique core in the centre of the molecule formed by two intersubunit disulfides and a single lysine residue from each monomer that is involved in intersubunit ionic interactions. The structure of this core protects the intersubunit disulfides from reduction, whereas the conserved intrasubunit disulfides are not formed in the reducing environment of the E. coli host cytosol. When oxidized to mimic the environment of the periplasmic space, TaCA has increased thermostability, retaining 90% activity after incubation at 70 degrees C for 1 h, making it a good candidate for industrial carbon-dioxide capture. The reduction of all TaCA cysteines resulted in dissociation of the tetrameric molecule into monomers with lower activity and reduced thermostability. Unlike other characterized alpha-carbonic anhydrases, TaCA does not display esterase activity towards p-nitrophenyl acetate, which appears to result from the increased rigidity of its protein scaffold.
-The structure of a tetrameric alpha-carbonic anhydrase from Thermovibrio ammonificans reveals a core formed around intermolecular disulfides that contribute to its thermostability.,James P, Isupov MN, Sayer C, Saneei V, Berg S, Lioliou M, Kotlar HK, Littlechild JA Acta Crystallogr D Biol Crystallogr. 2014 Oct 1;70(Pt 10):2607-18. doi:, 10.1107/S1399004714016526. Epub 2014 Sep 27. PMID:25286845<ref>PMID:25286845</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4c3t" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Carbonic anhydrase|Carbonic anhydrase]]
+*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Carbonate dehydratase]]
 [[Category: Large Structures]]
 [[Category: Thermovibrio ammonificans]]
-[[Category: Berg, S]]
+[[Category: Berg S]]
-[[Category: Isupov, M]]
+[[Category: Isupov M]]
-[[Category: James, P]]
+[[Category: James P]]
-[[Category: Kotlar, H]]
+[[Category: Kotlar H]]
-[[Category: Lioliou, M]]
+[[Category: Lioliou M]]
-[[Category: Littlechild, J]]
+[[Category: Littlechild J]]
-[[Category: Sayer, C]]
+[[Category: Sayer C]]
-[[Category: Acetazolamide]]
-[[Category: Carbon dioxide capture]]
-[[Category: Lyase]]
-[[Category: Thermal stability]]
-[[Category: Thermophilic]]

4c3t

From Proteopedia

Revision as of 17:24, 7 September 2022

The Carbonic anhydrase from Thermovibrio ammonificans reveals an interesting intermolecular disulfide contributing to increasing thermal stability of this enzyme

Structural highlights

Function

See Also

Contents

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