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1kdi

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Revision as of 05:15, 10 September 2015

REDUCED FORM OF PLASTOCYANIN FROM DRYOPTERIS CRASSIRHIZOMA

Structural highlights

1kdi is a 1 chain structure with sequence from Adiantum capillus-veneris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[PLAS_DRYCA] 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 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.

The structure and unusual pH dependence of plastocyanin from the fern Dryopteris crassirhizoma. The protonation of an active site histidine is hindered by pi-pi interactions.,Kohzuma T, Inoue T, Yoshizaki F, Sasakawa Y, Onodera K, Nagatomo S, Kitagawa T, Uzawa S, Isobe Y, Sugimura Y, Gotowda M, Kai Y J Biol Chem. 1999 Apr 23;274(17):11817-23. PMID:10206999^[1]

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

References

↑ Kohzuma T, Inoue T, Yoshizaki F, Sasakawa Y, Onodera K, Nagatomo S, Kitagawa T, Uzawa S, Isobe Y, Sugimura Y, Gotowda M, Kai Y. The structure and unusual pH dependence of plastocyanin from the fern Dryopteris crassirhizoma. The protonation of an active site histidine is hindered by pi-pi interactions. J Biol Chem. 1999 Apr 23;274(17):11817-23. PMID:10206999

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kdi"

@@ Line 4: / Line 4: @@
 <table><tr><td colspan='2'>[[1kdi]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KDI 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>
-<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=1kdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kdi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kdi RCSB], [http://www.ebi.ac.uk/pdbsum/1kdi 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=1kdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kdi OCA], [http://pdbe.org/1kdi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kdi RCSB], [http://www.ebi.ac.uk/pdbsum/1kdi PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1kdi" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1kdi

From Proteopedia

Revision as of 05:15, 10 September 2015

REDUCED FORM OF PLASTOCYANIN FROM DRYOPTERIS CRASSIRHIZOMA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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