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| | ==FNR-recruitment to the thylakoid== | | ==FNR-recruitment to the thylakoid== |
| - | <StructureSection load='3mhp' size='340' side='right' caption='[[3mhp]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='3mhp' size='340' side='right'caption='[[3mhp]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3mhp]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MHP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MHP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3mhp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MHP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MHP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qga|1qga]], [[1qg0|1qg0]], [[1qfz|1qfz]], [[1qfy|1qfy]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PETH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3888 Pisum sativum])</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=3mhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mhp OCA], [https://pdbe.org/3mhp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mhp RCSB], [https://www.ebi.ac.uk/pdbsum/3mhp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mhp ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferredoxin--NADP(+)_reductase Ferredoxin--NADP(+) reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.2 1.18.1.2] </span></td></tr>
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| - | <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=3mhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mhp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mhp RCSB], [http://www.ebi.ac.uk/pdbsum/3mhp PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FENR1_PEA FENR1_PEA]] May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power. | + | [https://www.uniprot.org/uniprot/FENR1_PEA FENR1_PEA] May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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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 3mhp" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Pisum sativum]] | | [[Category: Pisum sativum]] |
| - | [[Category: Alte, F]] | + | [[Category: Alte F]] |
| - | [[Category: Boelter, B]] | + | [[Category: Boelter B]] |
| - | [[Category: Groll, M]] | + | [[Category: Groll M]] |
| - | [[Category: Soll, J]] | + | [[Category: Soll J]] |
| - | [[Category: Fnr]]
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| - | [[Category: Oxidoreductase]]
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| - | [[Category: Poly proline ii helix]]
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| - | [[Category: Proton-flux]]
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| - | [[Category: Self assembly]]
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| - | [[Category: Thylakoid membrane]]
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| Structural highlights
Function
FENR1_PEA May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power.
Publication Abstract from PubMed
Ferredoxin:NADPH oxidoreductase (FNR) is a key enzyme of photosynthetic electron transport required for generation of reduction equivalents. Recently, two proteins were found to be involved in membrane-anchoring of FNR by specific interaction via a conserved Ser/Pro-rich motif: Tic62 and Trol. Our crystallographic study reveals that the FNR-binding motif, which forms a polyproline type II helix, induces self-assembly of two FNR monomers into a back-to-back dimer. Because binding occurs opposite to the FNR active sites, its activity is not affected by the interaction. Surface plasmon resonance analyses disclose a high affinity of FNR to the binding motif, which is strongly increased under acidic conditions. The pH of the chloroplast stroma changes dependent on the light conditions from neutral to slightly acidic in complete darkness or to alkaline at saturating light conditions. Recruiting of FNR to the thylakoids could therefore represent a regulatory mechanism to adapt FNR availability/activity to photosynthetic electron flow.
Ferredoxin:NADPH oxidoreductase is recruited to thylakoids by binding to a polyproline type II helix in a pH-dependent manner.,Alte F, Stengel A, Benz JP, Petersen E, Soll J, Groll M, Bolter B Proc Natl Acad Sci U S A. 2010 Nov 9;107(45):19260-5. Epub 2010 Oct 25. PMID:20974920[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Alte F, Stengel A, Benz JP, Petersen E, Soll J, Groll M, Bolter B. Ferredoxin:NADPH oxidoreductase is recruited to thylakoids by binding to a polyproline type II helix in a pH-dependent manner. Proc Natl Acad Sci U S A. 2010 Nov 9;107(45):19260-5. Epub 2010 Oct 25. PMID:20974920 doi:10.1073/pnas.1009124107
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