2pcf

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[[Image:2pcf.jpg|left|200px]]
 
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{{Structure
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==THE COMPLEX OF CYTOCHROME F AND PLASTOCYANIN DETERMINED WITH PARAMAGNETIC NMR. BASED ON THE STRUCTURES OF CYTOCHROME F AND PLASTOCYANIN, 10 STRUCTURES==
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|PDB= 2pcf |SIZE=350|CAPTION= <scene name='initialview01'>2pcf</scene>
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<StructureSection load='2pcf' size='340' side='right'caption='[[2pcf]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> and <scene name='pdbligand=HEC:HEME C'>HEC</scene>
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<table><tr><td colspan='2'>[[2pcf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bracm Bracm] and [https://en.wikipedia.org/wiki/Spiol Spiol]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PCF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PCF FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
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|GENE= PETE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3562 Spinacia oleracea]), PETE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3711 Brassica rapa])
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PETE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3562 SPIOL]), PETE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3711 BRACM])</td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pcf OCA], [https://pdbe.org/2pcf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pcf RCSB], [https://www.ebi.ac.uk/pdbsum/2pcf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pcf ProSAT]</span></td></tr>
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</table>
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'''THE COMPLEX OF CYTOCHROME F AND PLASTOCYANIN DETERMINED WITH PARAMAGNETIC NMR. BASED ON THE STRUCTURES OF CYTOCHROME F AND PLASTOCYANIN, 10 STRUCTURES'''
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== Function ==
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[[https://www.uniprot.org/uniprot/PLAS_SPIOL PLAS_SPIOL]] Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. [[https://www.uniprot.org/uniprot/CYF_BRARR CYF_BRARR]] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pc/2pcf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2pcf ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
BACKGROUND: The reduction of plastocyanin by cytochrome f is part of the chain of photosynthetic electron transfer reactions that links photosystems II and I. The reaction is rapid and is influenced by charged residues on both proteins. Previously determined structures show that the plastocyanin copper and cytochrome f haem redox centres are some distance apart from the relevant charged sidechains, and until now it was unclear how a transient electrostatic complex can be formed that brings the redox centres sufficiently close for a rapid reaction. RESULTS: A new approach was used to determine the structure of the transient complex between cytochrome f and plastocyanin. Diamagnetic chemical shift changes and intermolecular pseudocontact shifts in the NMR spectrum of plastocyanin were used as input in restrained rigid-body molecular dynamics calculations. An ensemble of ten structures was obtained, in which the root mean square deviation of the plastocyanin position relative to cytochrome f is 1.0 A. Electrostatic interaction is maintained at the same time as the hydrophobic side of plastocyanin makes close contact with the haem area, thus providing a short electron transfer pathway (Fe-Cu distance 10.9 A) via residues Tyr1 or Phe4 (cytochrome f) and the copper ligand His87 (plastocyanin). CONCLUSIONS: The combined use of diamagnetic and paramagnetic chemical shift changes makes it possible to obtain detailed information about the structure of a transient complex of redox proteins. The structure suggests that the electrostatic interactions 'guide' the partners into a position that is optimal for electron transfer, and which may be stabilised by short-range interactions.
BACKGROUND: The reduction of plastocyanin by cytochrome f is part of the chain of photosynthetic electron transfer reactions that links photosystems II and I. The reaction is rapid and is influenced by charged residues on both proteins. Previously determined structures show that the plastocyanin copper and cytochrome f haem redox centres are some distance apart from the relevant charged sidechains, and until now it was unclear how a transient electrostatic complex can be formed that brings the redox centres sufficiently close for a rapid reaction. RESULTS: A new approach was used to determine the structure of the transient complex between cytochrome f and plastocyanin. Diamagnetic chemical shift changes and intermolecular pseudocontact shifts in the NMR spectrum of plastocyanin were used as input in restrained rigid-body molecular dynamics calculations. An ensemble of ten structures was obtained, in which the root mean square deviation of the plastocyanin position relative to cytochrome f is 1.0 A. Electrostatic interaction is maintained at the same time as the hydrophobic side of plastocyanin makes close contact with the haem area, thus providing a short electron transfer pathway (Fe-Cu distance 10.9 A) via residues Tyr1 or Phe4 (cytochrome f) and the copper ligand His87 (plastocyanin). CONCLUSIONS: The combined use of diamagnetic and paramagnetic chemical shift changes makes it possible to obtain detailed information about the structure of a transient complex of redox proteins. The structure suggests that the electrostatic interactions 'guide' the partners into a position that is optimal for electron transfer, and which may be stabilised by short-range interactions.
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==About this Structure==
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The structure of the complex of plastocyanin and cytochrome f, determined by paramagnetic NMR and restrained rigid-body molecular dynamics.,Ubbink M, Ejdeback M, Karlsson BG, Bendall DS Structure. 1998 Mar 15;6(3):323-35. PMID:9551554<ref>PMID:9551554</ref>
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2PCF is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Brassica_rapa Brassica rapa] and [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PCF OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The structure of the complex of plastocyanin and cytochrome f, determined by paramagnetic NMR and restrained rigid-body molecular dynamics., Ubbink M, Ejdeback M, Karlsson BG, Bendall DS, Structure. 1998 Mar 15;6(3):323-35. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9551554 9551554]
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</div>
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[[Category: Brassica rapa]]
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<div class="pdbe-citations 2pcf" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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[[Category: Spinacia oleracea]]
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[[Category: Bendall, D S.]]
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[[Category: Ejdeback, M.]]
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[[Category: Karlsson, B G.]]
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[[Category: Ubbink, M.]]
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[[Category: CU]]
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[[Category: HEC]]
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[[Category: chemical shift]]
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[[Category: complex (electron transport proteins)]]
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[[Category: complex formation]]
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[[Category: dynamic complex]]
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[[Category: electron transport]]
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[[Category: paramagnetic]]
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[[Category: photosynthesis]]
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[[Category: pseudocontact shift]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:11:32 2008''
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==See Also==
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*[[Cytochrome f 3D structures|Cytochrome f 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bracm]]
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[[Category: Large Structures]]
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[[Category: Spiol]]
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[[Category: Bendall, D S]]
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[[Category: Ejdeback, M]]
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[[Category: Karlsson, B G]]
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[[Category: Ubbink, M]]
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[[Category: Chemical shift]]
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[[Category: Complex formation]]
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[[Category: Dynamic complex]]
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[[Category: Electron transport]]
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[[Category: Paramagnetic]]
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[[Category: Photosynthesis]]
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[[Category: Pseudocontact shift]]

Current revision

THE COMPLEX OF CYTOCHROME F AND PLASTOCYANIN DETERMINED WITH PARAMAGNETIC NMR. BASED ON THE STRUCTURES OF CYTOCHROME F AND PLASTOCYANIN, 10 STRUCTURES

PDB ID 2pcf

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