1bxv: Difference between revisions

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 <StructureSection load='1bxv' size='340' side='right'caption='[[1bxv]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1bxv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BXV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BXV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1bxv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_7942_=_FACHB-805 Synechococcus elongatus PCC 7942 = FACHB-805]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BXV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BXV 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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=1bxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bxv OCA], [http://pdbe.org/1bxv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bxv RCSB], [http://www.ebi.ac.uk/pdbsum/1bxv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bxv ProSAT]</span></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=1bxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bxv OCA], [https://pdbe.org/1bxv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bxv RCSB], [https://www.ebi.ac.uk/pdbsum/1bxv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bxv ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PLAS_SYNE7 PLAS_SYNE7]] Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I.
+[https://www.uniprot.org/uniprot/PLAS_SYNE7 PLAS_SYNE7] Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I.
 == Evolutionary Conservation ==
 [[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=1bxv ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The crystal structures of oxidized and reduced plastocyanins from Synechococcus sp. PCC 7942 have been determined at 1.9 and 1.8 A resolution, respectively, at pH 5.0. The protein consists of only 91 amino acid residues, the smallest number known for a plastocyanin, and apparently lacks the mostly conserved acidic patch that is believed to be important for recognition with electron-transfer partners. The protein has two acidic residues, Glu42 and Glu85, around Tyr83, which is thought to be a possible conduit for electrons, but these are neutralized by Arg88 and Lys58. Residue Arg88 interacts with Tyr83 through a pi-pi interaction in which the guanidinium group of the former completely overlaps the aromatic ring of the tyrosine. Reduction of the protein at pH 5.0 causes a lengthening of one Cu-N(His) bond by 0.36 A, despite the small rms deviation of 0.08 A calculated for the backbone atoms. Moreover, significant conformational changes of Arg88 and Lys58, along with the movement of a water molecule adjacent to the OH group of Tyr83, were observed on reduction; the guanidinium group of Arg88 rotates by more than 11 degrees, and the water molecule moves by 0.42 A. The changes around the copper site and the alterations around Tyr83 may be linked to the reduction of the copper.
-Crystal structure determinations of oxidized and reduced plastocyanin from the cyanobacterium Synechococcus sp. PCC 7942.,Inoue T, Sugawara H, Hamanaka S, Tsukui H, Suzuki E, Kohzuma T, Kai Y Biochemistry. 1999 May 11;38(19):6063-9. PMID:10320332<ref>PMID:10320332</ref>
+==See Also==
+*[[Plastocyanin 3D structures|Plastocyanin 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1bxv" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Hamanaka, S]]
+[[Category: Synechococcus elongatus PCC 7942 = FACHB-805]]
-[[Category: Inoue, T]]
+[[Category: Hamanaka S]]
-[[Category: Kai, Y]]
+[[Category: Inoue T]]
-[[Category: Kohzuma, T]]
+[[Category: Kai Y]]
-[[Category: Sugawara, H]]
+[[Category: Kohzuma T]]
-[[Category: Suzuki, E]]
+[[Category: Sugawara H]]
-[[Category: Tsukui, H]]
+[[Category: Suzuki E]]
-[[Category: Copper protein]]
+[[Category: Tsukui H]]
-[[Category: Electron transfer]]