1nw2: Difference between revisions
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==The crystal structure of the mutant R82E of Thioredoxin from Alicyclobacillus acidocaldarius== | ==The crystal structure of the mutant R82E of Thioredoxin from Alicyclobacillus acidocaldarius== | ||
<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=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1quw|1quw]], [[2trx|2trx]], [[1nsw|1nsw]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1quw|1quw]], [[2trx|2trx]], [[1nsw|1nsw]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </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=1nw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nw2 OCA], [http://pdbe.org/1nw2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nw2 RCSB], [http://www.ebi.ac.uk/pdbsum/1nw2 PDBsum]</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=1nw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nw2 OCA], [http://pdbe.org/1nw2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nw2 RCSB], [http://www.ebi.ac.uk/pdbsum/1nw2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nw2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nw/1nw2_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nw/1nw2_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1nw2" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1nw2" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:15, 7 February 2018
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
Function[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 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. References |
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