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==THIOREDOXIN H (OXIDIZED FORM), NMR, 23 STRUCTURES==
==THIOREDOXIN H (OXIDIZED FORM), NMR, 23 STRUCTURES==
<StructureSection load='1tof' size='340' side='right'caption='[[1tof]], [[NMR_Ensembles_of_Models | 23 NMR models]]' scene=''>
<StructureSection load='1tof' size='340' side='right'caption='[[1tof]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1tof]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlre Chlre]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TOF FirstGlance]. <br>
<table><tr><td colspan='2'>[[1tof]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TOF FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">THIOREDOXIN H CDNA (X78822 EMB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3055 CHLRE])</td></tr>
</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=1tof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tof OCA], [https://pdbe.org/1tof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tof RCSB], [https://www.ebi.ac.uk/pdbsum/1tof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tof ProSAT]</span></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=1tof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tof OCA], [https://pdbe.org/1tof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tof RCSB], [https://www.ebi.ac.uk/pdbsum/1tof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tof ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/TRXH_CHLRE TRXH_CHLRE]] Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The H form is known to activate a number of cytosolic enzymes.  
[https://www.uniprot.org/uniprot/TRXH_CHLRE TRXH_CHLRE] Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The H form is known to activate a number of cytosolic enzymes.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 19: Line 19:
</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=1tof ConSurf].
</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=1tof ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
NMR solution structures of a cytosolic plant thioredoxin h (112 amino acids, 11.7 kDa) from the green alga Chlamydonmonas reinhardtii have been calculated on the basis of 1904 NMR distance restraints, which include 90 distances used to restrain 45 hydrogen bonds, and 44 phi dihedral restraints. The structure of C. reinhardtii thioredoxin h was solved in its oxidised form, and the ensemble of 23 converged structures superpose to the geometric average structure with an atomic rmsd of 0.080 nm +/- 0.016 for the (N, C(alpha), C) backbone atoms of residues 4-110. Comparisons with other thioredoxins, such as thioredoxin from the bacterium Escherichia coli, thioredoxin 2 from a cyanobacterium of the Anabaena genus, and human thioredoxin, showed that thioredoxin h models share more structural features with human thioredoxin than with other bacterial thioredoxins. Examination of the accessible surface around the redoxactive peptide sequence indicates that a potent thioredoxin-h-substrate interaction could be similar to the vertebrate thioredoxin-substrate interactions.
NMR solution structure of an oxidised thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii.,Mittard V, Blackledge MJ, Stein M, Jacquot JP, Marion D, Lancelin JM Eur J Biochem. 1997 Jan 15;243(1-2):374-83. PMID:9030762<ref>PMID:9030762</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1tof" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Chlre]]
[[Category: Chlamydomonas reinhardtii]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Blackledge, M J]]
[[Category: Blackledge MJ]]
[[Category: Jacquot, J P]]
[[Category: Jacquot J-P]]
[[Category: Lancelin, J M]]
[[Category: Lancelin J-M]]
[[Category: Marion, D]]
[[Category: Marion D]]
[[Category: Mittard, V]]
[[Category: Mittard V]]
[[Category: Stein, M]]
[[Category: Stein M]]
[[Category: Electron transport]]
[[Category: Oxidoreductase]]

Revision as of 11:42, 1 May 2024

THIOREDOXIN H (OXIDIZED FORM), NMR, 23 STRUCTURESTHIOREDOXIN H (OXIDIZED FORM), NMR, 23 STRUCTURES

Structural highlights

1tof is a 1 chain structure with sequence from Chlamydomonas reinhardtii. 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

TRXH_CHLRE Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The H form is known to activate a number of cytosolic enzymes.

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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