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 [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1nw2]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_27009 Atcc 27009]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NW2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='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://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]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1nw2" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Atcc 27009]] | ||
[[Category: Thioredoxin-disulfide reductase]] | [[Category: Thioredoxin-disulfide reductase]] | ||
[[Category: Bartolucci, S]] | [[Category: Bartolucci, S]] | ||
Revision as of 08:36, 10 September 2015
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. See AlsoReferences |
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