1kdi
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1kdi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Adiantum_capillus-veneris Adiantum capillus-veneris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KDI FirstGlance]. <br> | <table><tr><td colspan='2'>[[1kdi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Adiantum_capillus-veneris Adiantum capillus-veneris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KDI FirstGlance]. <br> | ||
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</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=1kdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kdi OCA], [https://pdbe.org/1kdi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kdi RCSB], [https://www.ebi.ac.uk/pdbsum/1kdi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kdi ProSAT]</span></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=1kdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kdi OCA], [https://pdbe.org/1kdi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kdi RCSB], [https://www.ebi.ac.uk/pdbsum/1kdi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kdi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/PLAS_DRYCA PLAS_DRYCA] 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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</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=1kdi 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=1kdi ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Spectroscopic properties, amino acid sequence, electron transfer kinetics, and crystal structures of the oxidized (at 1.7 A resolution) and reduced form (at 1.8 A resolution) of a novel plastocyanin from the fern Dryopteris crassirhizoma are presented. Kinetic studies show that the reduced form of Dryopteris plastocyanin remains redox-active at low pH, under conditions where the oxidation of the reduced form of other plastocyanins is inhibited by the protonation of a solvent-exposed active site residue, His87 (equivalent to His90 in Dryopteris plastocyanin). The x-ray crystal structure analysis of Dryopteris plastocyanin reveals pi-pi stacking between Phe12 and His90, suggesting that the active site is uniquely protected against inactivation. Like higher plant plastocyanins, Dryopteris plastocyanin has an acidic patch, but this patch is located closer to the solvent-exposed active site His residue, and the total number of acidic residues is smaller. In the reactions of Dryopteris plastocyanin with inorganic redox reagents, the acidic patch (the "remote" site) and the hydrophobic patch surrounding His90 (the "adjacent" site) are equally efficient for electron transfer. These results indicate the significance of the lack of protonation at the active site of Dryopteris plastocyanin, the equivalence of the two electron transfer sites in this protein, and a possibility of obtaining a novel insight into the photosynthetic electron transfer system of the first vascular plant fern, including its molecular evolutionary aspects. This is the first report on the characterization of plastocyanin and the first three-dimensional protein structure from fern plant. | ||
| - | + | ==See Also== | |
| - | + | *[[Plastocyanin 3D structures|Plastocyanin 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Adiantum capillus-veneris]] | [[Category: Adiantum capillus-veneris]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Gotowda | + | [[Category: Gotowda M]] |
| - | [[Category: Hamada | + | [[Category: Hamada K]] |
| - | [[Category: Inoue | + | [[Category: Inoue T]] |
| - | [[Category: Kai | + | [[Category: Kai Y]] |
| - | [[Category: Kohzuma | + | [[Category: Kohzuma T]] |
| - | [[Category: Sugimura | + | [[Category: Sugimura Y]] |
| - | [[Category: Yoshizaki | + | [[Category: Yoshizaki F]] |
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Current revision
REDUCED FORM OF PLASTOCYANIN FROM DRYOPTERIS CRASSIRHIZOMA
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