1gaw
From Proteopedia
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|PDB= 1gaw |SIZE=350|CAPTION= <scene name='initialview01'>1gaw</scene>, resolution 2.20Å | |PDB= 1gaw |SIZE=350|CAPTION= <scene name='initialview01'>1gaw</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1gaq|1GAQ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gaw OCA], [http://www.ebi.ac.uk/pdbsum/1gaw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gaw RCSB]</span> | ||
}} | }} | ||
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[[Category: Kurisu, G.]] | [[Category: Kurisu, G.]] | ||
[[Category: Kusunoki, M.]] | [[Category: Kusunoki, M.]] | ||
| - | [[Category: FAD]] | ||
[[Category: oxidoreductase/electron transport]] | [[Category: oxidoreductase/electron transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:40:21 2008'' |
Revision as of 17:40, 30 March 2008
| |||||||
| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2 | ||||||
| Related: | 1GAQ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE ANALYSIS OF THE FERREDOXIN-NADP+ REDUCTASE FROM MAIZE LEAF
Overview
All 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.
About this Structure
1GAW is a Single protein structure of sequence from Zea mays. Full crystallographic information is available from OCA.
Reference
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
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