1iuz: Difference between revisions

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-[[Image:1iuz.jpg|left|200px]]
- {{Structure
+==PLASTOCYANIN==
-|PDB= 1iuz |SIZE=350|CAPTION= <scene name='initialview01'>1iuz</scene>, resolution 1.6&Aring;
+<StructureSection load='1iuz' size='340' side='right'caption='[[1iuz]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-|SITE= <scene name='pdbsite=COP:Cu+Binding+Site'>COP</scene>
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
+<table><tr><td colspan='2'>[[1iuz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ulva_pertusa Ulva pertusa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IUZ FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
-|GENE=
+<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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1iuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iuz OCA], [https://pdbe.org/1iuz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iuz RCSB], [https://www.ebi.ac.uk/pdbsum/1iuz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iuz ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PLAS_ULVPE PLAS_ULVPE] Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. Has antiviral activity against Potato virus Y (strain N).
+== 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/iu/1iuz_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/main_output.php?pdb_ID=1iuz ConSurf].
+<div style="clear:both"></div>
-'''PLASTOCYANIN'''
+==See Also==
+*[[Plastocyanin 3D structures|Plastocyanin 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-The crystal structure of plastocyanin from a green alga, Ulva pertusa, has been determined at 1.6-A resolution. At its copper site, U. pertusa plastocyanin has a distorted tetrahedral coordination geometry similar to other plastocyanins. In comparison with structures of plastocyanins reported formerly, a Cu(II)-Sdelta(Met92) bond distance (2.69 A) is shorter by about 0.2 A and a Cu(II)-Sgamma(Cys84) distance is longer by less than 0.1 A in U. pertusa plastocyanin. These subtle but significant differences are caused by the structural change at a His-Met loop (His87-Met92) due to an absence of a O(Asp85)-Ogamma(Ser88) hydrogen bond which is found in Enteromorpha prolifera plastocyanin. In addition, poplar and Chlamydomonas reinhardtii plastocyanins with a glutamine at residue 88 have a weak cation-pi interaction with Tyr83. This interaction lengthens the Cu(II)-Sdelta(Met92) bond of poplar and C. reinhardtii plastocyanins by 0.14 and 0.20 A, respectively. As a result of structural differences, U. pertusa plastocyanin has a less distorted geometry than the other plastocyanins. Thus, the cupric geometry is finely tuned by the interactions between residues 85 and 88 and between residues 83 and 88. This result implies that the copper site is more flexible than reported formerly and that the rack mechanism would be preferable to the entatic theory. The His-Met loop may regulate the electron transfer rate within the complex between plastocyanin and cytochrome f.
+[[Category: Large Structures]]
-==About this Structure==
-IUZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Ulva_pertusa Ulva pertusa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IUZ OCA].
-==Reference==
-Novel insight into the copper-ligand geometry in the crystal structure of Ulva pertusa plastocyanin at 1.6-A resolution. Structural basis for regulation of the copper site by residue 88., Shibata N, Inoue T, Nagano C, Nishio N, Kohzuma T, Onodera K, Yoshizaki F, Sugimura Y, Kai Y, J Biol Chem. 1999 Feb 12;274(7):4225-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9933621 9933621]
-[[Category: Single protein]]
 [[Category: Ulva pertusa]]
-[[Category: Shibata, N.]]
+[[Category: Shibata N]]
-[[Category: CU]]
-[[Category: SO4]]
-[[Category: electron transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:55:18 2008''