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[[Image:2pvd.jpg|left|200px]]<br /><applet load="2pvd" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2pvd, resolution 1.950&Aring;" />
'''Crystal srtucture of the reduced ferredoxin:thioredoxin reductase'''<br />


==Overview==
==Crystal srtucture of the reduced ferredoxin:thioredoxin reductase==
Oxygen-evolving photosynthetic organisms regulate carbon metabolism, through a light-dependent redox signalling pathway. Electrons are shuttled, from photosystem I by means of ferredoxin (Fdx) to ferredoxin-thioredoxin, reductase (FTR), which catalyses the two-electron-reduction of chloroplast, thioredoxins (Trxs). These modify target enzyme activities by reduction, regulating carbon flow. FTR is unique in its use of a [4Fe-4S] cluster and, a proximal disulphide bridge in the conversion of a light signal into a, thiol signal. We determined the structures of FTR in both its one- and its, two-electron-reduced intermediate states and of four complexes in the, pathway, including the ternary Fdx-FTR-Trx complex. Here we show that, in, the first complex (Fdx-FTR) of the pathway, the Fdx [2Fe-2S] cluster is, positioned suitably for electron transfer to the FTR [4Fe-4S] centre., After the transfer of one electron, an intermediate is formed in which one, sulphur atom of the FTR active site is free to attack a disulphide bridge, in Trx and the other sulphur atom forms a fifth ligand for an iron atom in, the FTR [4Fe-4S] centre--a unique structure in biology. Fdx then delivers, a second electron that cleaves the FTR-Trx heterodisulphide bond, which, occurs in the Fdx-FTR-Trx complex. In this structure, the redox centres of, the three proteins are aligned to maximize the efficiency of electron, transfer from the Fdx [2Fe-2S] cluster to the active-site disulphide of, Trxs. These results provide a structural framework for understanding the, mechanism of disulphide reduction by an iron-sulphur enzyme and describe, previously unknown interaction networks for both Fdx and Trx (refs 4-6).
<StructureSection load='2pvd' size='340' side='right'caption='[[2pvd]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2pvd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PVD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PVD 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]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2pvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pvd OCA], [https://pdbe.org/2pvd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pvd RCSB], [https://www.ebi.ac.uk/pdbsum/2pvd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pvd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FTRC_SYNY3 FTRC_SYNY3] Catalytic subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin.<ref>PMID:10649999</ref> <ref>PMID:14769790</ref> <ref>PMID:17611542</ref> <ref>PMID:19908864</ref>
== 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/pv/2pvd_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2pvd ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2PVD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=SF4:'>SF4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PVD OCA].
*[[Ferredoxin thioredoxin reductase|Ferredoxin thioredoxin reductase]]
 
== References ==
==Reference==
<references/>
Structural snapshots along the reaction pathway of ferredoxin-thioredoxin reductase., Dai S, Friemann R, Glauser DA, Bourquin F, Manieri W, Schurmann P, Eklund H, Nature. 2007 Jul 5;448(7149):92-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17611542 17611542]
__TOC__
[[Category: Protein complex]]
</StructureSection>
[[Category: Synechocystis sp.]]
[[Category: Large Structures]]
[[Category: Dai, S.]]
[[Category: Synechocystis sp]]
[[Category: SF4]]
[[Category: Dai S]]
[[Category: SO4]]
[[Category: iron-sulfur]]
[[Category: redox]]
[[Category: thioredoxin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:08:27 2008''

Latest revision as of 12:12, 21 February 2024

Crystal srtucture of the reduced ferredoxin:thioredoxin reductaseCrystal srtucture of the reduced ferredoxin:thioredoxin reductase

Structural highlights

2pvd is a 2 chain structure with sequence from Synechocystis sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.95Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FTRC_SYNY3 Catalytic subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin.[1] [2] [3] [4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Dai S, Schwendtmayer C, Schurmann P, Ramaswamy S, Eklund H. Redox signaling in chloroplasts: cleavage of disulfides by an iron-sulfur cluster. Science. 2000 Jan 28;287(5453):655-8. PMID:10649999
  2. ↑ Glauser DA, Bourquin F, Manieri W, Schürmann P. Characterization of ferredoxin:thioredoxin reductase modified by site-directed mutagenesis. J Biol Chem. 2004 Apr 16;279(16):16662-9. PMID:14769790 doi:10.1074/jbc.M313851200
  3. ↑ Dai S, Friemann R, Glauser DA, Bourquin F, Manieri W, Schurmann P, Eklund H. Structural snapshots along the reaction pathway of ferredoxin-thioredoxin reductase. Nature. 2007 Jul 5;448(7149):92-6. PMID:17611542 doi:http://dx.doi.org/10.1038/nature05937
  4. ↑ Xu X, Schürmann P, Chung JS, Hass MA, Kim SK, Hirasawa M, Tripathy JN, Knaff DB, Ubbink M. Ternary protein complex of ferredoxin, ferredoxin:thioredoxin reductase, and thioredoxin studied by paramagnetic NMR spectroscopy. J Am Chem Soc. 2009 Dec 9;131(48):17576-82. PMID:19908864 doi:10.1021/ja904205k

2pvd, resolution 1.95Å

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