1nw2: Difference between revisions
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<StructureSection load='1nw2' size='340' side='right'caption='[[1nw2]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1nw2' size='340' side='right'caption='[[1nw2]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1nw2]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1nw2]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius Alicyclobacillus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NW2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NW2 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1nw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nw2 OCA], [https://pdbe.org/1nw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nw2 RCSB], [https://www.ebi.ac.uk/pdbsum/1nw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nw2 ProSAT]</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=1nw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nw2 OCA], [https://pdbe.org/1nw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nw2 RCSB], [https://www.ebi.ac.uk/pdbsum/1nw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nw2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/THIO_ALIAC THIO_ALIAC] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Alicyclobacillus acidocaldarius]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Bartolucci S]] | ||
[[Category: | [[Category: De Simone G]] | ||
[[Category: Galdiero | [[Category: Galdiero S]] | ||
[[Category: Improta | [[Category: Improta R]] | ||
[[Category: Menchise | [[Category: Menchise V]] | ||
[[Category: Pedone | [[Category: Pedone C]] | ||
[[Category: Pedone | [[Category: Pedone E]] | ||
[[Category: Saviano | [[Category: Saviano M]] | ||
Revision as of 12:26, 16 August 2023
The crystal structure of the mutant R82E of Thioredoxin from Alicyclobacillus acidocaldariusThe crystal structure of the mutant R82E of Thioredoxin from Alicyclobacillus acidocaldarius
Structural highlights
FunctionTHIO_ALIAC Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe report a crystallographic and computational analysis of two mutant forms of the Alicyclobacillus acidocaldarius thioredoxin (BacTrx) done in order to evaluate the contribution of two specific amino acids to the thermostability of BacTrx. Our results suggest that the thermostability of BacTrx may be modulated by mutations affecting the overall electrostatic energy of the protein. An integrated structural and computational study of the thermostability of two thioredoxin mutants from Alicyclobacillus acidocaldarius.,Bartolucci S, De Simone G, Galdiero S, Improta R, Menchise V, Pedone C, Pedone E, Saviano M J Bacteriol. 2003 Jul;185(14):4285-9. PMID:12837806[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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