1go2: Difference between revisions

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-[[Image:1go2.png|left|200px]]
-<!--
+==Structure of Ferredoxin-NADP+ Reductase with Lys 72 replaced by Glu (K72E)==
-The line below this paragraph, containing "STRUCTURE_1go2", creates the "Structure Box" on the page.
+<StructureSection load='1go2' size='340' side='right'caption='[[1go2]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1go2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7119 Nostoc sp. PCC 7119]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GO2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GO2 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-{{STRUCTURE_1go2|  PDB=1go2  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1go2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1go2 OCA], [https://pdbe.org/1go2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1go2 RCSB], [https://www.ebi.ac.uk/pdbsum/1go2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1go2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FENR_NOSSO FENR_NOSSO]
+== 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/go/1go2_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=1go2 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The three-dimensional structures of K72E, K75R, K75S, K75Q, and K75E Anabaena Ferredoxin-NADP+ reductase (FNR) mutants have been solved, and particular structural details of these mutants have been used to assess the role played by residues 72 and 75 in optimal complex formation and electron transfer (ET) between FNR and its protein redox partners Ferredoxin (Fd) and Flavodoxin (Fld). Additionally, because there is no structural information available on the interaction between FNR and Fld, a model for the FNR:Fld complex has also been produced based on the previously reported crystal structures and on that of the rat Cytochrome P450 reductase (CPR), onto which FNR and Fld have been structurally aligned, and those reported for the Anabaena and maize FNR:Fd complexes. The model suggests putative electrostatic and hydrophobic interactions between residues on the FNR and Fld surfaces at the complex interface and provides an adequate orientation and distance between the FAD and FMN redox centers for efficient ET without the presence of any other molecule as electron carrier. Thus, the models now available for the FNR:Fd and FNR:Fld interactions and the structures presented here for the mutants at K72 and K75 in Anabaena FNR have been evaluated in light of previous biochemical data. These structures confirm the key participation of residue K75 and K72 in complex formation with both Fd and Fld. The drastic effect in FNR activity produced by replacement of K75 by Glu in the K75E FNR variant is explained not only by the observed changes in the charge distribution on the surface of the K75E FNR mutant, but also by the formation of a salt bridge interaction between E75 and K72 that simultaneously "neutralizes" two essential positive charged side chains for Fld/Fd recognition.
-===STRUCTURE OF FERREDOXIN-NADP+ REDUCTASE WITH LYS 72 REPLACED BY GLU (K72E)===
+Structural analysis of interactions for complex formation between Ferredoxin-NADP+ reductase and its protein partners.,Mayoral T, Martinez-Julvez M, Perez-Dorado I, Sanz-Aparicio J, Gomez-Moreno C, Medina M, Hermoso JA Proteins. 2005 May 15;59(3):592-602. PMID:15789405<ref>PMID:15789405</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_15789405}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1go2" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 15789405 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_15789405}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-[[1go2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Nostoc_sp._pcc_7119 Nostoc sp. pcc 7119]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GO2 OCA].
+[[Category: Nostoc sp. PCC 7119]]
+[[Category: Gomez-Moreno C]]
-==Reference==
+[[Category: Hermoso JA]]
-<ref group="xtra">PMID:15789405</ref><ref group="xtra">PMID:8890910</ref><references group="xtra"/>
+[[Category: Mayoral T]]
-[[Category: Nostoc sp. pcc 7119]]
+[[Category: Medina M]]
-[[Category: Gomez-Moreno, C.]]
+[[Category: Sanz-Aparicio J]]
-[[Category: Hermoso, J A.]]
-[[Category: Mayoral, T.]]
-[[Category: Medina, M.]]
-[[Category: Sanz-Aparicio, J.]]
-[[Category: Fad]]
-[[Category: Flavoprotein]]
-[[Category: Fnr]]
-[[Category: Nadp+ reductase]]
-[[Category: Oxidoreductase]]