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2puk
From Proteopedia
(Difference between revisions)
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<StructureSection load='2puk' size='340' side='right' caption='[[2puk]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='2puk' size='340' side='right' caption='[[2puk]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2puk]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <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> |
</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"><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">[[2pu9|2pu9]]</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 | + | <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='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://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'>[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> |
</table> | </table> | ||
== Function == | == 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/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). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 2puk" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Cyanobacterium synechocystis]] |
| - | [[Category: | + | [[Category: Spiol]] |
[[Category: Dai, S]] | [[Category: Dai, S]] | ||
[[Category: Eklund, H]] | [[Category: Eklund, H]] | ||
Revision as of 20:29, 9 September 2015
Crystal structure of the binary complex between ferredoxin: thioredoxin reductase and thioredoxin m
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