2f51: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
(12 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2f51.gif|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_2f51", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_2f51|  PDB=2f51  |  SCENE=  }}
'''Structure of Trichomonas vaginalis thioredoxin'''


==Structure of Trichomonas vaginalis thioredoxin==
<StructureSection load='2f51' size='340' side='right'caption='[[2f51]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
</table>
== Function ==
[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.


==Overview==
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>
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.


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


==Reference==
==See Also==
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]
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
[[Category: Single protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[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 Sun May  4 03:28:02 2008''

Latest revision as of 09:06, 6 November 2024

Structure of Trichomonas vaginalis thioredoxin

2f51, resolution 1.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2f51&oldid=4255958"