2f51

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(New page: 200px<br /><applet load="2f51" size="350" color="white" frame="true" align="right" spinBox="true" caption="2f51, resolution 1.90&Aring;" /> '''Structure of Trichom...)
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[[Image:2f51.gif|left|200px]]<br /><applet load="2f51" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2f51, resolution 1.90&Aring;" />
 
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'''Structure of Trichomonas vaginalis thioredoxin'''<br />
 
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==Overview==
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==Structure of Trichomonas vaginalis thioredoxin==
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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.
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<StructureSection load='2f51' size='340' side='right'caption='[[2f51]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8IEV4_TRIVA Q8IEV4_TRIVA]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f5/2f51_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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2F51 is a [http://en.wikipedia.org/wiki/Single_protein 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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16421453 16421453]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 2f51" style="background-color:#fffaf0;"></div>
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[[Category: Trichomonas vaginalis]]
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[[Category: Alphey, M.S.]]
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[[Category: Hunter, W.N.]]
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[[Category: Iulek, J.]]
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[[Category: thioredoxin fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:27:45 2008''
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==See Also==
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*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Trichomonas vaginalis]]
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[[Category: Alphey MS]]
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[[Category: Hunter WN]]
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[[Category: Iulek J]]

Current revision

Structure of Trichomonas vaginalis thioredoxin

PDB ID 2f51

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