1xob: Difference between revisions

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New page: left|200px<br /><applet load="1xob" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xob" /> '''THIOREDOXIN (REDUCED DITHIO FORM), NMR, 20 S...
 
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[[Image:1xob.jpg|left|200px]]<br /><applet load="1xob" size="450" color="white" frame="true" align="right" spinBox="true"
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'''THIOREDOXIN (REDUCED DITHIO FORM), NMR, 20 STRUCTURES'''<br />


==Overview==
==THIOREDOXIN (REDUCED DITHIO FORM), NMR, 20 STRUCTURES==
BACKGROUND: Thioredoxin participates in thiol-disulfide exchange reactions, and both oxidized thioredoxin (disulfide form) and reduced thioredoxin, (dithiol form) are found under physiological conditions. Previous, structural studies suggested that the two forms were extremely similar, although significant functional and spectroscopic differences exist. We, therefore undertook high-resolution solution structural studies of the two, forms of Escherichia coli thioredoxin in order to detect subtle, conformational differences. RESULTS: The solution structures of reduced, and oxidized thioredoxin are extremely similar. Backbone structure is, largely identical in the two forms, with slight differences in the region, of the active site, which includes Cys32 and Cys35. The side chain sulfur, atom of Cys32 is tilted away from that of Cys35 in the reduced form of the, protein to accommodate the increase in S-S distance that occurs upon, reduction of the disulfide, but the chi 1 angles of the two cysteines, remain the same in the two forms. CONCLUSIONS: Only subtle conformational, changes occur upon changing the oxidation state of the active site, cysteines, including the positions of some side chains and in hydrogen, bonding patterns in the active site region. Functional differences between, the two forms are probably therefore related to differences in local, conformational flexibility in and near the active site loop.
<StructureSection load='1xob' size='340' side='right'caption='[[1xob]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1xob]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1trx 1trx]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XOB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XOB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1xob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xob OCA], [https://pdbe.org/1xob PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xob RCSB], [https://www.ebi.ac.uk/pdbsum/1xob PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xob ProSAT]</span></td></tr>
</table>
== 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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xo/1xob_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xob ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1XOB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure superseeds the now removed PDB entry 1TRX. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XOB OCA].
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin., Jeng MF, Campbell AP, Begley T, Holmgren A, Case DA, Wright PE, Dyson HJ, Structure. 1994 Sep 15;2(9):853-68. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7812718 7812718]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Begley, T.]]
[[Category: Begley T]]
[[Category: Campbell, A.P.]]
[[Category: Campbell AP]]
[[Category: Case, D.A.]]
[[Category: Case DA]]
[[Category: Dyson, H.J.]]
[[Category: Dyson HJ]]
[[Category: Holmgren, A.]]
[[Category: Holmgren A]]
[[Category: Jeng, M.F.]]
[[Category: Jeng M-F]]
[[Category: Wright, P.E.]]
[[Category: Wright PE]]
[[Category: electron transport]]
[[Category: redox-active center]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:14:03 2007''

Latest revision as of 09:36, 1 May 2024

THIOREDOXIN (REDUCED DITHIO FORM), NMR, 20 STRUCTURESTHIOREDOXIN (REDUCED DITHIO FORM), NMR, 20 STRUCTURES

Structural highlights

1xob is a 1 chain structure with sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1trx. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

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