1gaw: Difference between revisions
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<StructureSection load='1gaw' size='340' side='right'caption='[[1gaw]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1gaw' size='340' side='right'caption='[[1gaw]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1gaw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1gaw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GAW FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
<tr id=' | <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></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=1gaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gaw OCA], [https://pdbe.org/1gaw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gaw RCSB], [https://www.ebi.ac.uk/pdbsum/1gaw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gaw ProSAT]</span></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=1gaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gaw OCA], [https://pdbe.org/1gaw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gaw RCSB], [https://www.ebi.ac.uk/pdbsum/1gaw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gaw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9SLP6_MAIZE Q9SLP6_MAIZE] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Zea mays]] | ||
[[Category: Hase | [[Category: Hase T]] | ||
[[Category: Kurisu | [[Category: Kurisu G]] | ||
[[Category: Kusunoki | [[Category: Kusunoki M]] | ||
Latest revision as of 02:29, 28 December 2023
CRYSTAL STRUCTURE ANALYSIS OF THE FERREDOXIN-NADP+ REDUCTASE FROM MAIZE LEAFCRYSTAL STRUCTURE ANALYSIS OF THE FERREDOXIN-NADP+ REDUCTASE FROM MAIZE LEAF
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAll oxygenic photosynthetically derived reducing equivalents are utilized by combinations of a single multifuctional electron carrier protein, ferredoxin (Fd), and several Fd-dependent oxidoreductases. We report the first crystal structure of the complex between maize leaf Fd and Fd-NADP(+) oxidoreductase (FNR). The redox centers in the complex--the 2Fe-2S cluster of Fd and flavin adenine dinucleotide (FAD) of FNR--are in close proximity; the shortest distance is 6.0 A. The intermolecular interactions in the complex are mainly electrostatic, occurring through salt bridges, and the interface near the prosthetic groups is hydrophobic. NMR experiments on the complex in solution confirmed the FNR recognition sites on Fd that are identified in the crystal structure. Interestingly, the structures of Fd and FNR in the complex and in the free state differ in several ways. For example, in the active site of FNR, Fd binding induces the formation of a new hydrogen bond between side chains of Glu 312 and Ser 96 of FNR. We propose that this type of molecular communication not only determines the optimal orientation of the two proteins for electron transfer, but also contributes to the modulation of the enzymatic properties of FNR. Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase.,Kurisu G, Kusunoki M, Katoh E, Yamazaki T, Teshima K, Onda Y, Kimata-Ariga Y, Hase T Nat Struct Biol. 2001 Feb;8(2):117-21. PMID:11175898[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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