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2pvo

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Revision as of 11:21, 11 September 2015

Crystal srtucture of the ternary complex between thioredoxin f, ferredoxin, and ferredoxin: thioredoxin reductase

Structural highlights

2pvo is a 4 chain structure with sequence from Cyanobacterium synechocystis and Spiol. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	2pu9, 2puk, 2puo, 2pvd, 2pvg
Gene:	ftrC (Cyanobacterium synechocystis), ftrV (Cyanobacterium synechocystis), petF, fed (Cyanobacterium synechocystis)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[FER_SYNY3] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. [Q55389_SYNY3] FTR is a [4Fe-4S] protein playing a central role in the ferredoxin/thioredoxin regulatory chain. It converts an electron signal (photoreduced ferredoxin) to a thiol signal (reduced thioredoxin) in the regulation of enzymes by reduction of specific disulfide groups. Catalyzes the light-dependent activation of several photosynthetic enzymes (By similarity).[PIRNR:PIRNR000260] [TRXF_SPIOL] Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The F form is known to activate a number of enzymes of the photosynthetic carbon cycle. [FTRV_SYNY3] FTR is a [4Fe-4S] protein playing a central role in the ferredoxin/thioredoxin regulatory chain. It converts an electron signal (photoreduced ferredoxin) to a thiol signal (reduced thioredoxin) in the regulation of enzymes by reduction of specific disulfide groups. Catalyzes the light-dependent activation of several photosynthetic enzymes (By similarity).

Evolutionary Conservation

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

Publication Abstract from PubMed

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).

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:17611542^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2pvo"

@@ Line 2: / Line 2: @@
 <StructureSection load='2pvo' size='340' side='right' caption='[[2pvo]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2pvo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea] and [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PVO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PVO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2pvo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cyanobacterium_synechocystis Cyanobacterium synechocystis] and [http://en.wikipedia.org/wiki/Spiol Spiol]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PVO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PVO FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pu9|2pu9]], [[2puk|2puk]], [[2puo|2puo]], [[2pvd|2pvd]], [[2pvg|2pvg]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ftrC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp.]), ftrV ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp.]), petF, fed ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp.])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ftrC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Cyanobacterium synechocystis]), ftrV ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Cyanobacterium synechocystis]), petF, fed ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Cyanobacterium synechocystis])</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=2pvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pvo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pvo RCSB], [http://www.ebi.ac.uk/pdbsum/2pvo PDBsum]</span></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=2pvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pvo OCA], [http://pdbe.org/2pvo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pvo RCSB], [http://www.ebi.ac.uk/pdbsum/2pvo PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FER_SYNY3 FER_SYNY3]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. [[http://www.uniprot.org/uniprot/TRXF_SPIOL TRXF_SPIOL]] Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The F form is known to activate a number of enzymes of the photosynthetic carbon cycle. [[http://www.uniprot.org/uniprot/FTRV_SYNY3 FTRV_SYNY3]] FTR is a [4Fe-4S] protein playing a central role in the ferredoxin/thioredoxin regulatory chain. It converts an electron signal (photoreduced ferredoxin) to a thiol signal (reduced thioredoxin) in the regulation of enzymes by reduction of specific disulfide groups. Catalyzes the light-dependent activation of several photosynthetic enzymes (By similarity).
+[[http://www.uniprot.org/uniprot/FER_SYNY3 FER_SYNY3]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. [[http://www.uniprot.org/uniprot/Q55389_SYNY3 Q55389_SYNY3]] FTR is a [4Fe-4S] protein playing a central role in the ferredoxin/thioredoxin regulatory chain. It converts an electron signal (photoreduced ferredoxin) to a thiol signal (reduced thioredoxin) in the regulation of enzymes by reduction of specific disulfide groups. Catalyzes the light-dependent activation of several photosynthetic enzymes (By similarity).[PIRNR:PIRNR000260] [[http://www.uniprot.org/uniprot/TRXF_SPIOL TRXF_SPIOL]] Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The F form is known to activate a number of enzymes of the photosynthetic carbon cycle. [[http://www.uniprot.org/uniprot/FTRV_SYNY3 FTRV_SYNY3]] FTR is a [4Fe-4S] protein playing a central role in the ferredoxin/thioredoxin regulatory chain. It converts an electron signal (photoreduced ferredoxin) to a thiol signal (reduced thioredoxin) in the regulation of enzymes by reduction of specific disulfide groups. Catalyzes the light-dependent activation of several photosynthetic enzymes (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2pvo" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 36: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Spinacia oleracea]]
+[[Category: Cyanobacterium synechocystis]]
-[[Category: Synechocystis sp]]
+[[Category: Spiol]]
 [[Category: Dai, S]]
 [[Category: Electron transport]]

2pvo

From Proteopedia

Revision as of 11:21, 11 September 2015

Crystal srtucture of the ternary complex between thioredoxin f, ferredoxin, and ferredoxin: thioredoxin reductase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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