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| | <StructureSection load='1pcs' size='340' side='right'caption='[[1pcs]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='1pcs' size='340' side='right'caption='[[1pcs]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1pcs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aphanocapsa_sp._(strain_n-1) Aphanocapsa sp. (strain n-1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PCS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1pcs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PCS 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></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]] 2.15Å</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=1pcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pcs OCA], [http://pdbe.org/1pcs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pcs RCSB], [http://www.ebi.ac.uk/pdbsum/1pcs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pcs ProSAT]</span></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></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=1pcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pcs OCA], [https://pdbe.org/1pcs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pcs RCSB], [https://www.ebi.ac.uk/pdbsum/1pcs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pcs ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PLAS_SYNY3 PLAS_SYNY3]] Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I.[HAMAP-Rule:MF_00566] | + | [https://www.uniprot.org/uniprot/PLAS_SYNY3 PLAS_SYNY3] Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I.[HAMAP-Rule:MF_00566] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1pcs" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1pcs" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Plastocyanin 3D structures|Plastocyanin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cerda, B De La]] | + | [[Category: Synechocystis sp. PCC 6803]] |
| - | [[Category: Hervas, M]] | + | [[Category: De La Cerda B]] |
| - | [[Category: Navarro, J A]] | + | [[Category: De La Rosa MA]] |
| - | [[Category: Romero, A]] | + | [[Category: Hervas M]] |
| - | [[Category: Rosa, M A.De La]]
| + | [[Category: Navarro JA]] |
| - | [[Category: Varela, P F]] | + | [[Category: Romero A]] |
| - | [[Category: Electron transport]] | + | [[Category: Varela PF]] |
| - | [[Category: Plastocyanin]] | + | |
| Structural highlights
Function
PLAS_SYNY3 Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I.[HAMAP-Rule:MF_00566]
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
The crystal structure of the triple mutant A42D/D47P/A63L plastocyanin from the cyanobacterium Synechocystis sp. PCC 6803 has been determined by Patterson search methods using the known structure of the poplar protein. Crystals of the triple mutant A42D/D47P/A63L, which are stable for days in its oxidized form, were grown from ammonium sulfate, with the cell constants a = b = 34.3 A and c = 111.8 A belonging to space group P3(2)21. The structure was refined using restrained crystallographic refinement to an R-factor of 16.7% for 4070 independent reflections between 8.0 and 2.15 A with intensities greater than 2 sigma (I), with root mean square deviations of 0.013 A and 1.63 degrees from ideal bond lengths and bond angles, respectively. The final model comprises 727 non-hydrogen protein atoms within 98 residues, 75 water molecules and a single copper ion. The overall tertiary fold of Synechocystis plastocyanin consists of a compact ellipsoidal beta-sandwich structure made up of two beta-sheets embracing a hydrophobic core. Each sheet contains parallel and antiparallel beta-strands. In addition to the beta-sheets, the structure contains an alpha-helix from Pro47 to Lys54 that follows beta-strand 4. The three-dimensional structure of Synechocystis plastocyanin is thus similar to those reported for the copper protein isolated from eukaryotic organisms and, in particular, from the cyanobacterium Anabaena variabilis, the only cyanobacterial plastocyanin structure available so far. The molecule holds an hydrophobic region surrounding His87, as do other plastocyanins, but the lack of negatively charged residues at the putative distant remote site surrounding Tyr83 could explain why the Synechocystis protein exhibits a collisional reaction mechanism for electron transfer to photosystem I (PSI), which involves no formation of the transient plastocyanin-PSI complex kinetically observed in green algae and higher plants.
The 2.15 A crystal structure of a triple mutant plastocyanin from the cyanobacterium Synechocystis sp. PCC 6803.,Romero A, De la Cerda B, Varela PF, Navarro JA, Hervas M, De la Rosa MA J Mol Biol. 1998 Jan 16;275(2):327-36. PMID:9466912[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Romero A, De la Cerda B, Varela PF, Navarro JA, Hervas M, De la Rosa MA. The 2.15 A crystal structure of a triple mutant plastocyanin from the cyanobacterium Synechocystis sp. PCC 6803. J Mol Biol. 1998 Jan 16;275(2):327-36. PMID:9466912 doi:10.1006/jmbi.1997.1455
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