2oe0: Difference between revisions

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[[Image:2oe0.jpg|left|200px]]


{{Structure
==Crystal Structure of Mitochondrial Thioredoxin 3 from Saccharomyces cerevisiae==
|PDB= 2oe0 |SIZE=350|CAPTION= <scene name='initialview01'>2oe0</scene>, resolution 2.00&Aring;
<StructureSection load='2oe0' size='340' side='right'caption='[[2oe0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[2oe0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OE0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OE0 FirstGlance]. <br>
|ACTIVITY=  
</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&#8491;</td></tr>
|GENE= TRX3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2oe0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oe0 OCA], [https://pdbe.org/2oe0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oe0 RCSB], [https://www.ebi.ac.uk/pdbsum/2oe0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oe0 ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=[[2oe1|2OE1]], [[2oe3|2OE3]]
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2oe0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oe0 OCA], [http://www.ebi.ac.uk/pdbsum/2oe0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2oe0 RCSB]</span>
[https://www.uniprot.org/uniprot/TRX3_YEAST TRX3_YEAST]
}}
== 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/oe/2oe0_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2oe0 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The yeast Saccharomyces cerevisiae Trx3 is a key member of the thioredoxin system to control the cellular redox homeostasis in mitochondria. We solved the crystal structures of yeast Trx3 in oxidized and reduced forms at 1.80 and 2.10 A, respectively. Besides the active site, the additional cysteine residue Cys69 also undergoes a significant redox-correlated conformational change. Comparative structural analyses in combination with activity assays revealed that residue Cys69 could be S-nitrosylated in vitro. S-nitrosylation of Cys69 will decrease the activity of Trx3 by 20%, which is comparable to the effect of the Cys69Ser mutation. Taken together, these findings provided us some new insights into the putative function of the additional cysteine residues of Trx3.


'''Crystal Structure of Mitochondrial Thioredoxin 3 from Saccharomyces cerevisiae'''
Structural and mechanistic analyses of yeast mitochondrial thioredoxin Trx3 reveal putative function of its additional cysteine residues.,Bao R, Zhang Y, Zhou CZ, Chen Y Biochim Biophys Acta. 2009 Apr;1794(4):716-21. Epub 2009 Jan 3. PMID:19166985<ref>PMID:19166985</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2oe0" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
2OE0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OE0 OCA].
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Bao R]]
[[Category: Bao, R.]]
[[Category: Chen YX]]
[[Category: Chen, Y X.]]
[[Category: Zhang YR]]
[[Category: Zhang, Y R.]]
[[Category: Zhou CZ]]
[[Category: Zhou, C Z.]]
[[Category: alpha/beta sandwich]]
[[Category: dimer]]
[[Category: electron transport]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:16:26 2008''

Latest revision as of 10:44, 9 October 2024

Crystal Structure of Mitochondrial Thioredoxin 3 from Saccharomyces cerevisiaeCrystal Structure of Mitochondrial Thioredoxin 3 from Saccharomyces cerevisiae

Structural highlights

2oe0 is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRX3_YEAST

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 PubMed

The yeast Saccharomyces cerevisiae Trx3 is a key member of the thioredoxin system to control the cellular redox homeostasis in mitochondria. We solved the crystal structures of yeast Trx3 in oxidized and reduced forms at 1.80 and 2.10 A, respectively. Besides the active site, the additional cysteine residue Cys69 also undergoes a significant redox-correlated conformational change. Comparative structural analyses in combination with activity assays revealed that residue Cys69 could be S-nitrosylated in vitro. S-nitrosylation of Cys69 will decrease the activity of Trx3 by 20%, which is comparable to the effect of the Cys69Ser mutation. Taken together, these findings provided us some new insights into the putative function of the additional cysteine residues of Trx3.

Structural and mechanistic analyses of yeast mitochondrial thioredoxin Trx3 reveal putative function of its additional cysteine residues.,Bao R, Zhang Y, Zhou CZ, Chen Y Biochim Biophys Acta. 2009 Apr;1794(4):716-21. Epub 2009 Jan 3. PMID:19166985[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Bao R, Zhang Y, Zhou CZ, Chen Y. Structural and mechanistic analyses of yeast mitochondrial thioredoxin Trx3 reveal putative function of its additional cysteine residues. Biochim Biophys Acta. 2009 Apr;1794(4):716-21. Epub 2009 Jan 3. PMID:19166985 doi:S1570-9639(08)00400-7

2oe0, resolution 2.00Å

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