1oow: Difference between revisions
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<StructureSection load='1oow' size='340' side='right'caption='[[1oow]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1oow' size='340' side='right'caption='[[1oow]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1oow]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1oow]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OOW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OOW 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]] 2Å</td></tr> | ||
<tr id=' | <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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oow OCA], [https://pdbe.org/1oow PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oow RCSB], [https://www.ebi.ac.uk/pdbsum/1oow PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oow ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/PLAS_SPIOL PLAS_SPIOL] 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]] | ||
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</div> | </div> | ||
<div class="pdbe-citations 1oow" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1oow" 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: | [[Category: Spinacia oleracea]] | ||
[[Category: Ejdeback | [[Category: Ejdeback M]] | ||
[[Category: Hansson | [[Category: Hansson O]] | ||
[[Category: Jacobson | [[Category: Jacobson F]] | ||
[[Category: Jansson | [[Category: Jansson H]] | ||
[[Category: Okvist | [[Category: Okvist M]] | ||
[[Category: Sjolin | [[Category: Sjolin L]] | ||
Latest revision as of 12:30, 16 August 2023
The crystal structure of the spinach plastocyanin double mutant G8D/L12E gives insight into its low reactivity towards photosystem 1 and cytochrome fThe crystal structure of the spinach plastocyanin double mutant G8D/L12E gives insight into its low reactivity towards photosystem 1 and cytochrome f
Structural highlights
FunctionPLAS_SPIOL Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. 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 PubMedPlastocyanin (Pc) is a copper-containing protein, which functions as an electron carrier between the cytochrome b(6)f and photosystem 1 (PS1) complexes in the photosynthetic electron transfer (ET) chain. The ET is mediated by His87 situated in the hydrophobic surface in the north region of Pc. Also situated in this region is Leu12, which mutated to other amino acids severely disturbs the ET from cytochrome f and to PS1, indicating the importance of the hydrophobic surface. The crystal structure of the Pc double mutant G8D/L12E has been determined to 2.0 A resolution, with a crystallographic R-factor of 18.3% (R(free)=23.2%). A comparison with the wild-type structure reveals that structural differences are limited to the sites of the mutations. In particular, there is a small but significant change in the hydrophobic surface close to His87. Evidently, this leads to a mismatch in the reactive complex with the redox partners. For PS1 this results in a 20 times weaker binding and an eightfold slower ET as determined by kinetic measurements. The mutations that have been introduced do not affect the optical absorption spectrum. However, there is a small change in the EPR spectrum, which can be related to changes in the copper coordination geometry. The crystal structure of the spinach plastocyanin double mutant G8D/L12E gives insight into its low reactivity towards photosystem 1 and cytochrome f.,Jansson H, Okvist M, Jacobson F, Ejdeback M, Hansson O, Sjolin L Biochim Biophys Acta. 2003 Dec 8;1607(2-3):203-10. PMID:14670610[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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