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[[Image:2f51.gif|left|200px]]


{{Structure
==Structure of Trichomonas vaginalis thioredoxin==
|PDB= 2f51 |SIZE=350|CAPTION= <scene name='initialview01'>2f51</scene>, resolution 1.90&Aring;
<StructureSection load='2f51' size='340' side='right'caption='[[2f51]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[2f51]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichomonas_vaginalis Trichomonas vaginalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F51 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F51 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]] 1.9&#8491;</td></tr>
|GENE= trx ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5722 Trichomonas vaginalis])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2f51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f51 OCA], [https://pdbe.org/2f51 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f51 RCSB], [https://www.ebi.ac.uk/pdbsum/2f51 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f51 ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f51 OCA], [http://www.ebi.ac.uk/pdbsum/2f51 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f51 RCSB]</span>
[https://www.uniprot.org/uniprot/Q8IEV4_TRIVA Q8IEV4_TRIVA]
}}
== 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/f5/2f51_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=2f51 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of thioredoxin from the anaerobic organism Trichomonas vaginalis (TvTrx) has been determined at 1.9 angstroms resolution. The structure is that of a typical thioredoxin: a five-stranded beta-sheet structure with two alpha-helices on either side. The active site of the protein carries a Trp-Cys-Gly-Pro-Cys motif, residues 34-38, at the N-terminus of an alpha-helix (alpha2). The cysteine residues in this motif form a redox-active disulfide necessary for thioredoxin activity. With high-resolution data available, it was possible to model numerous amino-acid side chains in alternate conformations and this includes the redox-active disulfide cysteine residues. The sample was initially in the oxidized state and the use of X-rays from an intense third-generation synchrotron source resulted in partial photoreduction of this labile redox centre. Comparisons with previously determined thioredoxin structures indicate that TvTrx is most similar to the human homologue, although the insertion of three residues between strands beta4 and beta5 makes the corresponding turn longer and more flexible in TvTrx. In addition, three significant amino-acid differences are identified on the protein surfaces near to the active-site Cys35. These residues may contribute to the interactions that specific thioredoxins form with their cognate physiological partners.


'''Structure of Trichomonas vaginalis thioredoxin'''
High-resolution structure of recombinant Trichomonas vaginalis thioredoxin.,Iulek J, Alphey MS, Westrop GD, Coombs GH, Hunter WN Acta Crystallogr D Biol Crystallogr. 2006 Feb;62(Pt 2):216-20. Epub 2006, Jan 18. PMID:16421453<ref>PMID:16421453</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2f51" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
The structure of thioredoxin from the anaerobic organism Trichomonas vaginalis (TvTrx) has been determined at 1.9 angstroms resolution. The structure is that of a typical thioredoxin: a five-stranded beta-sheet structure with two alpha-helices on either side. The active site of the protein carries a Trp-Cys-Gly-Pro-Cys motif, residues 34-38, at the N-terminus of an alpha-helix (alpha2). The cysteine residues in this motif form a redox-active disulfide necessary for thioredoxin activity. With high-resolution data available, it was possible to model numerous amino-acid side chains in alternate conformations and this includes the redox-active disulfide cysteine residues. The sample was initially in the oxidized state and the use of X-rays from an intense third-generation synchrotron source resulted in partial photoreduction of this labile redox centre. Comparisons with previously determined thioredoxin structures indicate that TvTrx is most similar to the human homologue, although the insertion of three residues between strands beta4 and beta5 makes the corresponding turn longer and more flexible in TvTrx. In addition, three significant amino-acid differences are identified on the protein surfaces near to the active-site Cys35. These residues may contribute to the interactions that specific thioredoxins form with their cognate physiological partners.
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
 
== References ==
==About this Structure==
<references/>
2F51 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Trichomonas_vaginalis Trichomonas vaginalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F51 OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
High-resolution structure of recombinant Trichomonas vaginalis thioredoxin., Iulek J, Alphey MS, Westrop GD, Coombs GH, Hunter WN, Acta Crystallogr D Biol Crystallogr. 2006 Feb;62(Pt 2):216-20. Epub 2006, Jan 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16421453 16421453]
[[Category: Single protein]]
[[Category: Trichomonas vaginalis]]
[[Category: Trichomonas vaginalis]]
[[Category: Alphey, M S.]]
[[Category: Alphey MS]]
[[Category: Hunter, W N.]]
[[Category: Hunter WN]]
[[Category: Iulek, J.]]
[[Category: Iulek J]]
[[Category: thioredoxin fold]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:58:00 2008''

Latest revision as of 09:06, 6 November 2024

Structure of Trichomonas vaginalis thioredoxin

2f51, resolution 1.90Å

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