1dj7

From Proteopedia

(Difference between revisions)

Current revision

CRYSTAL STRUCTURE OF FERREDOXIN THIOREDOXIN REDUCTASE

Structural highlights

1dj7 is a 2 chain structure with sequence from Synechocystis sp. PCC 6803. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.6Å
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.

Publication Abstract from PubMed

Light generates reducing equivalents in chloroplasts that are used not only for carbon reduction, but also for the regulation of the activity of chloroplast enzymes by reduction of regulatory disulfides via the ferredoxin:thioredoxin reductase (FTR) system. FTR, the key electron/thiol transducer enzyme in this pathway, is unique in that it can reduce disulfides by an iron-sulfur cluster, a property that is explained by the tight contact of its active-site disulfide and the iron-sulfur center. The thin, flat FTR molecule makes the two-electron reduction possible by forming on one side a mixed disulfide with thioredoxin and by providing on the opposite side access to ferredoxin for delivering electrons.

Redox signaling in chloroplasts: cleavage of disulfides by an iron-sulfur cluster.,Dai S, Schwendtmayer C, Schurmann P, Ramaswamy S, Eklund H Science. 2000 Jan 28;287(5453):655-8. PMID:10649999^[5]

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

References

↑ 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
↑ 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
↑ 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
↑ 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
↑ 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

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/1dj7"

@@ Line 3: / Line 3: @@
 <StructureSection load='1dj7' size='340' side='right'caption='[[1dj7]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1dj7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aphanocapsa_sp._(strain_n-1) Aphanocapsa sp. (strain n-1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DJ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DJ7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1dj7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DJ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DJ7 FirstGlance]. <br>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1dj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dj7 OCA], [https://pdbe.org/1dj7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dj7 RCSB], [https://www.ebi.ac.uk/pdbsum/1dj7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dj7 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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).
+[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]]
@@ Line 14: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dj/1dj7_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 36: / Line 37: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Dai, S]]
+[[Category: Synechocystis sp. PCC 6803]]
-[[Category: Eklund, H]]
+[[Category: Dai S]]
-[[Category: Ramaswamy, S]]
+[[Category: Eklund H]]
-[[Category: Schurmann, P]]
+[[Category: Ramaswamy S]]
-[[Category: Schwendtmayer, C]]
+[[Category: Schurmann P]]
-[[Category: 4fe-4s cluster binding fold with cxcx16cxcx8cxc binding motif]]
+[[Category: Schwendtmayer C]]
-[[Category: Electron transport]]

1dj7

From Proteopedia

Current revision

CRYSTAL STRUCTURE OF 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

Personal tools

Navigation

Search

Toolbox