2plt: Difference between revisions

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[[Image:2plt.png|left|200px]]
==STRUCTURE DETERMINATION OF PLASTOCYANIN FROM A CRYSTAL SPECIMEN WITH HEMIHEDRAL TWINNING FRACTION OF ONE-HALF==
<StructureSection load='2plt' size='340' side='right' caption='[[2plt]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2plt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PLT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PLT FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene><br>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2plt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2plt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2plt RCSB], [http://www.ebi.ac.uk/pdbsum/2plt PDBsum]</span></td></tr>
<table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pl/2plt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of plastocyanin from the green alga Chlamydomonas reinhardtii has been determined at 1.5-A resolution with a crystallographic R factor of 16.8%. Plastocyanin is a small (98 amino acids), blue copper-binding protein that catalyzes the transfer of electrons in oxygenic photosynthesis from cytochrome f in the quinol oxidase complex to P700+ in photosystem I. Chlamydomonas reinhardtii plastocyanin is an eight-stranded, antiparallel beta-barrel with a single copper atom coordinated in quasitetrahedral geometry by two imidazole nitrogens (from His-37 and His-87), a cysteine sulfur (from Cys-84), and a methionine sulfur (from Met-92). The molecule contains a region of negative charge surrounding Tyr-83 (the putative distant site of electron transfer) and an exclusively hydrophobic region surrounding His-87; these regions are thought to be involved in the recognition of reaction partners for the purpose of directing electron transfer. Chlamydomonas reinhardtii plastocyanin is similar to the other plastocyanins of known structure, particularly the green algal plastocyanins from Enteromorpha prolifera and Scenedesmus obliquus. A potential "through-bond" path of electron transfer has been identified in the protein that involves the side chain of Tyr-83, the main-chain atoms between residues 83 and 84, the side chain of Cys-84, the copper atom, and the side chain of His-87.


{{STRUCTURE_2plt|  PDB=2plt  |  SCENE=  }}
The 1.5-A crystal structure of plastocyanin from the green alga Chlamydomonas reinhardtii.,Redinbo MR, Cascio D, Choukair MK, Rice D, Merchant S, Yeates TO Biochemistry. 1993 Oct 12;32(40):10560-7. PMID:8399201<ref>PMID:8399201</ref>


===STRUCTURE DETERMINATION OF PLASTOCYANIN FROM A CRYSTAL SPECIMEN WITH HEMIHEDRAL TWINNING FRACTION OF ONE-HALF===
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_8399201}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[2plt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PLT OCA].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:008399201</ref><ref group="xtra">PMID:015299512</ref><references group="xtra"/>
[[Category: Chlamydomonas reinhardtii]]
[[Category: Chlamydomonas reinhardtii]]
[[Category: Merchant, S.]]
[[Category: Merchant, S.]]

Revision as of 12:40, 21 May 2014

STRUCTURE DETERMINATION OF PLASTOCYANIN FROM A CRYSTAL SPECIMEN WITH HEMIHEDRAL TWINNING FRACTION OF ONE-HALFSTRUCTURE DETERMINATION OF PLASTOCYANIN FROM A CRYSTAL SPECIMEN WITH HEMIHEDRAL TWINNING FRACTION OF ONE-HALF

Structural highlights

2plt is a 1 chain structure with sequence from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, RCSB, PDBsum

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 plastocyanin from the green alga Chlamydomonas reinhardtii has been determined at 1.5-A resolution with a crystallographic R factor of 16.8%. Plastocyanin is a small (98 amino acids), blue copper-binding protein that catalyzes the transfer of electrons in oxygenic photosynthesis from cytochrome f in the quinol oxidase complex to P700+ in photosystem I. Chlamydomonas reinhardtii plastocyanin is an eight-stranded, antiparallel beta-barrel with a single copper atom coordinated in quasitetrahedral geometry by two imidazole nitrogens (from His-37 and His-87), a cysteine sulfur (from Cys-84), and a methionine sulfur (from Met-92). The molecule contains a region of negative charge surrounding Tyr-83 (the putative distant site of electron transfer) and an exclusively hydrophobic region surrounding His-87; these regions are thought to be involved in the recognition of reaction partners for the purpose of directing electron transfer. Chlamydomonas reinhardtii plastocyanin is similar to the other plastocyanins of known structure, particularly the green algal plastocyanins from Enteromorpha prolifera and Scenedesmus obliquus. A potential "through-bond" path of electron transfer has been identified in the protein that involves the side chain of Tyr-83, the main-chain atoms between residues 83 and 84, the side chain of Cys-84, the copper atom, and the side chain of His-87.

The 1.5-A crystal structure of plastocyanin from the green alga Chlamydomonas reinhardtii.,Redinbo MR, Cascio D, Choukair MK, Rice D, Merchant S, Yeates TO Biochemistry. 1993 Oct 12;32(40):10560-7. PMID:8399201[1]

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

References

  1. ↑ Redinbo MR, Cascio D, Choukair MK, Rice D, Merchant S, Yeates TO. The 1.5-A crystal structure of plastocyanin from the green alga Chlamydomonas reinhardtii. Biochemistry. 1993 Oct 12;32(40):10560-7. PMID:8399201

2plt, resolution 1.50Å

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