3cvb
From Proteopedia
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==Regulation of Protein Function: Crystal Packing Interfaces and Conformational Dimerization== | ==Regulation of Protein Function: Crystal Packing Interfaces and Conformational Dimerization== | ||
| - | <StructureSection load='3cvb' size='340' side='right' caption='[[3cvb]], [[Resolution|resolution]] 1.40Å' scene=''> | + | <StructureSection load='3cvb' size='340' side='right'caption='[[3cvb]], [[Resolution|resolution]] 1.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3cvb]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3cvb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Phormidium_laminosum Phormidium laminosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CVB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CVB FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene></td></tr> | |
| - | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cvb OCA], [https://pdbe.org/3cvb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cvb RCSB], [https://www.ebi.ac.uk/pdbsum/3cvb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cvb ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/PLAS_PHOLA PLAS_PHOLA] Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cv/3cvb_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cv/3cvb_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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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=3cvb ConSurf]. | </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=3cvb ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The accepted view of interprotein electron transport involves molecules diffusing between donor and acceptor redox sites. An emerging alternative hypothesis is that efficient long-range electron transport can be achieved through proteins arranged in supramolecular assemblies. In this study, we have investigated the crystal packing interfaces in three crystal forms of plastocyanin, an integral component of the photosynthetic electron transport chain, and discuss their potential relevance to in vivo supramolecular assemblies. Symmetry-related protein chains within these crystals have Cu-Cu separations of <25 A, a distance that readily supports electron transfer. In one structure, the plastocyanin molecule exists in two forms in which a backbone displacement coupled with side chain rearrangements enables the modulation of protein-protein interfaces. | ||
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| - | Regulation of Protein Function: Crystal Packing Interfaces and Conformational Dimerization.,Crowley PB, Matias PM, Mi H, Firbank SJ, Banfield MJ, Dennison C Biochemistry. 2008 May 15;. PMID:18479147<ref>PMID:18479147</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Plastocyanin 3D structures|Plastocyanin 3D structures]] | |
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| - | == | + | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Banfield | + | [[Category: Phormidium laminosum]] |
| - | [[Category: Crowley | + | [[Category: Banfield MJ]] |
| - | [[Category: Dennison | + | [[Category: Crowley PB]] |
| - | [[Category: Firbank | + | [[Category: Dennison C]] |
| - | [[Category: Matias | + | [[Category: Firbank SJ]] |
| - | [[Category: Mi | + | [[Category: Matias PM]] |
| - | + | [[Category: Mi H]] | |
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Current revision
Regulation of Protein Function: Crystal Packing Interfaces and Conformational Dimerization
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