6i19
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Chlamydomonas reinhardtii thioredoxin h1== | |
| + | <StructureSection load='6i19' size='340' side='right' caption='[[6i19]], [[Resolution|resolution]] 1.38Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6i19]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I19 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I19 FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6i19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i19 OCA], [http://pdbe.org/6i19 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i19 RCSB], [http://www.ebi.ac.uk/pdbsum/6i19 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i19 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Protein disulfide reduction by thioredoxins (TRXs) controls the conformation of enzyme active sites and their multimeric complex formation. TRXs are small oxidoreductases that are broadly conserved in all living organisms. In photosynthetic eukaryotes, TRXs form a large multigenic family, and they have been classified in different types: f, m, x, y, and z types are chloroplastic, while o and h types are located in mitochondria and cytosol. In the model unicellular alga Chlamydomonas reinhardtii, the TRX family contains seven types, with f- and h-types represented by two isozymes. Type-f TRXs interact specifically with targets in the chloroplast, controlling photosynthetic carbon fixation by the Calvin(-)Benson cycle. We solved the crystal structures of TRX f2 and TRX h1 from C. reinhardtii. The systematic comparison of their atomic features revealed a specific conserved electropositive crown around the active site of TRX f, complementary to the electronegative surface of their targets. We postulate that this surface provides specificity to each type of TRX. | ||
| - | + | Crystal Structure of Chloroplastic Thioredoxin f2 from Chlamydomonas reinhardtii Reveals Distinct Surface Properties.,Lemaire SD, Tedesco D, Crozet P, Michelet L, Fermani S, Zaffagnini M, Henri J Antioxidants (Basel). 2018 Nov 23;7(12). pii: antiox7120171. doi:, 10.3390/antiox7120171. PMID:30477165<ref>PMID:30477165</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6i19" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Crozet, P]] | ||
[[Category: Fermani, S]] | [[Category: Fermani, S]] | ||
| - | [[Category: | + | [[Category: Henri, J]] |
| + | [[Category: Lemaire, S D]] | ||
[[Category: Michelet, L]] | [[Category: Michelet, L]] | ||
[[Category: Tedesco, D]] | [[Category: Tedesco, D]] | ||
| - | [[Category: | + | [[Category: Zaffagnini, M]] |
| - | [[Category: | + | [[Category: Electron transport]] |
| - | [[Category: | + | [[Category: H-type cytosolic thioredoxin oxidized]] |
Revision as of 06:48, 5 December 2018
Crystal structure of Chlamydomonas reinhardtii thioredoxin h1
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