2pvd

From Proteopedia

(Difference between revisions)

Revision as of 15:33, 17 June 2021

Crystal srtucture of the reduced ferredoxin:thioredoxin reductase

Structural highlights

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

Function

[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] [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/2pvd"

@@ Line 1: / Line 1: @@
 ==Crystal srtucture of the reduced ferredoxin:thioredoxin reductase==
-<StructureSection load='2pvd' size='340' side='right' caption='[[2pvd]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+<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 [http://en.wikipedia.org/wiki/Cyanobacterium_synechocystis Cyanobacterium synechocystis]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PVD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2pvd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cyanobacterium_synechocystis Cyanobacterium synechocystis]. 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pu9|2pu9]], [[2puk|2puk]], [[2puo|2puo]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2pu9|2pu9]], [[2puk|2puk]], [[2puo|2puo]]</div></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])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ftrC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Cyanobacterium synechocystis]), ftrV ([https://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=2pvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pvd OCA], [http://pdbe.org/2pvd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pvd RCSB], [http://www.ebi.ac.uk/pdbsum/2pvd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pvd 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=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 ==
-[[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/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).
+[[https://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] [[https://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]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pv/2pvd_consurf.spt"</scriptWhenChecked>
+    <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>
@@ Line 30: / Line 30: @@
 </div>
 <div class="pdbe-citations 2pvd" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Ferredoxin thioredoxin reductase|Ferredoxin thioredoxin reductase]]
 == References ==
 <references/>
@@ Line 35: / Line 38: @@
 </StructureSection>
 [[Category: Cyanobacterium synechocystis]]
+[[Category: Large Structures]]
 [[Category: Dai, S]]
 [[Category: Electron transport]]

2pvd

From Proteopedia

Revision as of 15:33, 17 June 2021

Crystal srtucture of the reduced ferredoxin:thioredoxin reductase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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