2pcf

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(Difference between revisions)

Revision as of 12:37, 11 September 2015

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

Structural highlights

2pcf is a 2 chain structure with sequence from Bracm and Spiol. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	PETE (SPIOL), PETE (BRACM)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[PLAS_SPIOL] Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. [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.

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

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.

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^[1]

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

References

↑ Ubbink M, Ejdeback M, Karlsson BG, Bendall DS. The structure of the complex of plastocyanin and cytochrome f, determined by paramagnetic NMR and restrained rigid-body molecular dynamics. Structure. 1998 Mar 15;6(3):323-35. PMID:9551554

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/2pcf"

@@ Line 2: / Line 2: @@
 <StructureSection load='2pcf' size='340' side='right' caption='[[2pcf]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2pcf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Brassica_rapa Brassica rapa] and [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PCF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2pcf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bracm Bracm] and [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PCF FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">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])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PETE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3562 SPIOL]), PETE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3711 BRACM])</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=2pcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pcf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pcf RCSB], [http://www.ebi.ac.uk/pdbsum/2pcf 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=2pcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pcf OCA], [http://pdbe.org/2pcf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pcf RCSB], [http://www.ebi.ac.uk/pdbsum/2pcf PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PLAS_SPIOL PLAS_SPIOL]] Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. [[http://www.uniprot.org/uniprot/CYF_BRARA CYF_BRARA]] 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 (By similarity).
+[[http://www.uniprot.org/uniprot/PLAS_SPIOL PLAS_SPIOL]] Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. [[http://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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2pcf" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 34: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Brassica rapa]]
+[[Category: Bracm]]
-[[Category: Spinacia oleracea]]
+[[Category: Spiol]]
 [[Category: Bendall, D S]]
 [[Category: Ejdeback, M]]

2pcf

From Proteopedia

Revision as of 12:37, 11 September 2015

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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