5hr1: Difference between revisions
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<StructureSection load='5hr1' size='340' side='right'caption='[[5hr1]], [[Resolution|resolution]] 2.14Å' scene=''> | <StructureSection load='5hr1' size='340' side='right'caption='[[5hr1]], [[Resolution|resolution]] 2.14Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5hr1]] is a 7 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5hr1]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HR1 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]] 2.144Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=5hr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hr1 OCA], [https://pdbe.org/5hr1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hr1 RCSB], [https://www.ebi.ac.uk/pdbsum/5hr1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hr1 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/THIO_ECOLI THIO_ECOLI] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli O157:H7]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cousido-Siah | [[Category: Cousido-Siah A]] | ||
[[Category: Howard | [[Category: Howard EI]] | ||
[[Category: Mitschler | [[Category: Mitschler A]] | ||
[[Category: Noguera | [[Category: Noguera ME]] | ||
[[Category: Podjarny | [[Category: Podjarny A]] | ||
[[Category: Santos | [[Category: Santos J]] | ||
[[Category: Vazquez | [[Category: Vazquez DS]] | ||
Latest revision as of 13:51, 16 August 2023
Crystal structure of thioredoxin L107A mutantCrystal structure of thioredoxin L107A mutant
Structural highlights
FunctionTHIO_ECOLI Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Publication Abstract from PubMedThioredoxin is a ubiquitous small protein that catalyzes redox reactions of protein thiols. Additionally, thioredoxin from E. coli (EcTRX) is a widely-used model for structure-function studies. In a previous paper, we characterized several single-point mutants of the C-terminal helix (CTH) that alter global stability of EcTRX. However, spectroscopic signatures and enzymatic activity for some of these mutants were found essentially unaffected. A comprehensive structural characterization at the atomic level of these near-invariant mutants can provide detailed information about structural variability of EcTRX. We address this point through the determination of the crystal structures of four point-mutants, whose mutations occurs within or near the CTH, namely L94A, E101G, N106A and L107A. These structures are mostly unaffected compared with the wild-type variant. Notably, the E101G mutant presents a large region with two alternative traces for the backbone of the same chain. It represents a significant shift in backbone positions. Enzymatic activity measurements and conformational dynamics studies monitored by NMR and molecular dynamic simulations show that E101G mutation results in a small effect in the structural features of the protein. We hypothesize that these alternative conformations represent samples of the native-state ensemble of EcTRX, specifically the magnitude and location of conformational heterogeneity. Structural variability of E. coli thioredoxin captured in the crystal structures of single-point mutants.,Noguera ME, Vazquez DS, Ferrer-Sueta G, Agudelo WA, Howard E, Rasia RM, Manta B, Cousido-Siah A, Mitschler A, Podjarny A, Santos J Sci Rep. 2017 Feb 9;7:42343. doi: 10.1038/srep42343. PMID:28181556[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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