2puk: Difference between revisions

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 ==Crystal structure of the binary complex between ferredoxin: thioredoxin reductase and thioredoxin m==
-<StructureSection load='2puk' size='340' side='right' caption='[[2puk]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+<StructureSection load='2puk' size='340' side='right'caption='[[2puk]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2puk]] is a 6 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=2PUK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PUK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2puk]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Spiol Spiol] and [https://en.wikipedia.org/wiki/Synechocystis_sp Synechocystis sp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PUK 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></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></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pu9|2pu9]]</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]]</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 Synechocystis sp]), ftrV ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp])</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=2puk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2puk OCA], [http://pdbe.org/2puk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2puk RCSB], [http://www.ebi.ac.uk/pdbsum/2puk PDBsum]</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=2puk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2puk OCA], [https://pdbe.org/2puk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2puk RCSB], [https://www.ebi.ac.uk/pdbsum/2puk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2puk 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/TRXM_SPIOL TRXM_SPIOL]] Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The M form is known to activate NADP-malate dehydrogenase. [[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/TRXM_SPIOL TRXM_SPIOL]] Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The M form is known to activate NADP-malate dehydrogenase. [[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/pu/2puk_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pu/2puk_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=2puk ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 32: / Line 33: @@
 ==See Also==
 *[[Ferredoxin thioredoxin reductase|Ferredoxin thioredoxin reductase]]
-*[[Thioredoxin|Thioredoxin]]
+*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Cyanobacterium synechocystis]]
+[[Category: Large Structures]]
 [[Category: Spiol]]
+[[Category: Synechocystis sp]]
 [[Category: Dai, S]]
 [[Category: Eklund, H]]