1gjr: Difference between revisions

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-[[Image:1gjr.gif|left|200px]]<br />
-<applet load="1gjr" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1gjr, resolution 2.1&Aring;" />
-'''FERREDOXIN-NADP+ REDUCTASE COMPLEXED WITH NADP+ BY COCRYSTALLIZATION'''<br />
-==Overview==
+==Ferredoxin-NADP+ Reductase complexed with NADP+ by COCRYSTALLIZATION==
-The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyses the production, of NADPH in photosynthesis. The three-dimensional structure of FNR, presents two distinct domains, one for binding of the FAD prosthetic group, and the other for NADP+ binding. In spite of extensive experiments and, different crystallographic approaches, many aspects about how the NADP+, substrate binds to FNR and how the hydride ion is transferred from FAD to, NADP+ remain unclear. The structure of an FNR:NADP+ complex from Anabaena, has been determined by X-ray diffraction analysis of the cocrystallised, units to 2.1 A resolution. Structural perturbation of FNR induced by, complex formation produces a narrower cavity in which the 2'-phospho-AMP, and pyrophosphate portions of the NADP+ are perfectly bound. In ... [[http://ispc.weizmann.ac.il/pmbin/getpm?12079352 (full description)]]
+<StructureSection load='1gjr' size='340' side='right'caption='[[1gjr]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1gjr]] 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=1GJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GJR FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#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=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=1gjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjr OCA], [https://pdbe.org/1gjr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gjr RCSB], [https://www.ebi.ac.uk/pdbsum/1gjr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gjr 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/gj/1gjr_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=1gjr ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyses the production of NADPH in photosynthesis. The three-dimensional structure of FNR presents two distinct domains, one for binding of the FAD prosthetic group and the other for NADP+ binding. In spite of extensive experiments and different crystallographic approaches, many aspects about how the NADP+ substrate binds to FNR and how the hydride ion is transferred from FAD to NADP+ remain unclear. The structure of an FNR:NADP+ complex from Anabaena has been determined by X-ray diffraction analysis of the cocrystallised units to 2.1 A resolution. Structural perturbation of FNR induced by complex formation produces a narrower cavity in which the 2'-phospho-AMP and pyrophosphate portions of the NADP+ are perfectly bound. In addition, the nicotinamide mononucleotide moiety is placed in a new pocket created near the FAD cofactor with the ribose being in a tight conformation. The crystal structure of this FNR:NADP+ complex obtained by cocrystallisation displays NADP+ in an unusual conformation and can be considered as an intermediate state in the process of coenzyme recognition and binding. Structural analysis and comparison with previously reported complexes allow us to postulate a mechanism which would permit efficient hydride transfer to occur. Besides, this structure gives new insights into the postulated formation of the ferredoxin:FNR:NADP+ ternary complex by prediction of new intermolecular interactions, which could only exist after FNR:NADP+ complex formation. Finally, structural comparison with the members of the broad FNR structural family also provides an explanation for the high specificity exhibited by FNR for NADP+/H versus NAD+/H.
-==About this Structure==
+Mechanism of coenzyme recognition and binding revealed by crystal structure analysis of ferredoxin-NADP+ reductase complexed with NADP+.,Hermoso JA, Mayoral T, Faro M, Gomez-Moreno C, Sanz-Aparicio J, Medina M J Mol Biol. 2002 Jun 21;319(5):1133-42. PMID:12079352<ref>PMID:12079352</ref>
-GJR is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.]] with FAD and NAP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Ferredoxin--NADP(+)_reductase Ferredoxin--NADP(+) reductase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.2 1.18.1.2]]. Structure known Active Site: FAD. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GJR OCA]].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Mechanism of coenzyme recognition and binding revealed by crystal structure analysis of ferredoxin-NADP+ reductase complexed with NADP+., Hermoso JA, Mayoral T, Faro M, Gomez-Moreno C, Sanz-Aparicio J, Medina M, J Mol Biol. 2002 Jun 21;319(5):1133-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12079352 12079352]
+</div>
-[[Category: Anabaena sp.]]
+<div class="pdbe-citations 1gjr" style="background-color:#fffaf0;"></div>
-[[Category: Ferredoxin--NADP(+) reductase]]
+== References ==
-[[Category: Single protein]]
+<references/>
-[[Category: Gomez-Moreno, C.]]
+__TOC__
-[[Category: Hermoso, J.A.]]
+</StructureSection>
-[[Category: Mayoral, T.]]
+[[Category: Large Structures]]
-[[Category: Medina, M.]]
+[[Category: Nostoc sp. PCC 7119]]
-[[Category: Sanz-Aparicio, J.]]
+[[Category: Gomez-Moreno C]]
-[[Category: FAD]]
+[[Category: Hermoso JA]]
-[[Category: NAP]]
+[[Category: Mayoral T]]
-[[Category: fad]]
+[[Category: Medina M]]
-[[Category: flavoprotein]]
+[[Category: Sanz-Aparicio J]]
-[[Category: fnr]]
-[[Category: nadp]]
-[[Category: nadp reductase]]
-[[Category: oxidoreductase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:23:55 2007''