1fnc: Difference between revisions

Revision as of 13:40, 21 February 2008

REFINED CRYSTAL STRUCTURE OF SPINACH FERREDOXIN REDUCTASE AT 1.7 ANGSTROMS RESOLUTION: OXIDIZED, REDUCED, AND 2'-PHOSPHO-5'-AMP BOUND STATES

OverviewOverview

The crystal structure of spinach ferredoxin-NADP(+)-oxidoreductase (FNR), determined by multiple isomorphous replacement at 2.6 A resolution, has been refined at 1.7 A resolution to an R-factor of 17.9%. The structure of FNR bound to the competitive inhibitor 2'-phospho-5'-AMP (P-AMP) has also been refined at 1.7 A to an R-factor of 17.4% and dithionite-reduced/P-AMP-bound FNR has been refined at 2.0 A to an R-factor of 14.9%. The P-AMP-bound structure was used to construct a model for the binding of NADP+. Over 200 solvation sites were included in each structure, and many of the best defined solvation sites stabilize buried turns. A bulk solvent correction obviated the need for a low-resolution data cutoff. An acidic side-chain likely to be responsible for the low pH requirement for crystallization has been identified. Three large networks of the hydrophobic side-chains help define the FNR structure. One of these contains a large cavity far from the active site, which coincides with the lone site of sequence heterogeneity in FNR, and may provide a site for membrane attachment. The reduced structure shows that Ser96 moves toward atom N-5 of FAD and a water molecule moves toward atom N-1 of FAD, while the flavin moiety remains planar. Possible sources of a proton that must be picked up upon reduction are discussed.

About this StructureAbout this Structure

1FNC is a Single protein structure of sequence from Spinacia oleracea with , and as ligands. Active as Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2 Full crystallographic information is available from OCA.

ReferenceReference

Refined crystal structure of spinach ferredoxin reductase at 1.7 A resolution: oxidized, reduced and 2'-phospho-5'-AMP bound states., Bruns CM, Karplus PA, J Mol Biol. 1995 Mar 17;247(1):125-45. PMID:7897656

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-[[Image:1fnc.gif|left|200px]]<br /><applet load="1fnc" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1fnc.gif|left|200px]]<br /><applet load="1fnc" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1fnc, resolution 2.0&Aring;" />
 '''REFINED CRYSTAL STRUCTURE OF SPINACH FERREDOXIN REDUCTASE AT 1.7 ANGSTROMS RESOLUTION: OXIDIZED, REDUCED, AND 2'-PHOSPHO-5'-AMP BOUND STATES'''<br />
 ==Overview==
-The crystal structure of spinach ferredoxin-NADP(+)-oxidoreductase (FNR), determined by multiple isomorphous replacement at 2.6 A resolution, has, been refined at 1.7 A resolution to an R-factor of 17.9%. The structure of, FNR bound to the competitive inhibitor 2'-phospho-5'-AMP (P-AMP) has also, been refined at 1.7 A to an R-factor of 17.4% and, dithionite-reduced/P-AMP-bound FNR has been refined at 2.0 A to an, R-factor of 14.9%. The P-AMP-bound structure was used to construct a model, for the binding of NADP+. Over 200 solvation sites were included in each, structure, and many of the best defined solvation sites stabilize buried, turns. A bulk solvent correction obviated the need for a low-resolution, data cutoff. An acidic side-chain likely to be responsible for the low pH, requirement for crystallization has been identified. Three large networks, of the hydrophobic side-chains help define the FNR structure. One of these, contains a large cavity far from the active site, which coincides with the, lone site of sequence heterogeneity in FNR, and may provide a site for, membrane attachment. The reduced structure shows that Ser96 moves toward, atom N-5 of FAD and a water molecule moves toward atom N-1 of FAD, while, the flavin moiety remains planar. Possible sources of a proton that must, be picked up upon reduction are discussed.
+The crystal structure of spinach ferredoxin-NADP(+)-oxidoreductase (FNR), determined by multiple isomorphous replacement at 2.6 A resolution, has been refined at 1.7 A resolution to an R-factor of 17.9%. The structure of FNR bound to the competitive inhibitor 2'-phospho-5'-AMP (P-AMP) has also been refined at 1.7 A to an R-factor of 17.4% and dithionite-reduced/P-AMP-bound FNR has been refined at 2.0 A to an R-factor of 14.9%. The P-AMP-bound structure was used to construct a model for the binding of NADP+. Over 200 solvation sites were included in each structure, and many of the best defined solvation sites stabilize buried turns. A bulk solvent correction obviated the need for a low-resolution data cutoff. An acidic side-chain likely to be responsible for the low pH requirement for crystallization has been identified. Three large networks of the hydrophobic side-chains help define the FNR structure. One of these contains a large cavity far from the active site, which coincides with the lone site of sequence heterogeneity in FNR, and may provide a site for membrane attachment. The reduced structure shows that Ser96 moves toward atom N-5 of FAD and a water molecule moves toward atom N-1 of FAD, while the flavin moiety remains planar. Possible sources of a proton that must be picked up upon reduction are discussed.
 ==About this Structure==
-FNC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea] with SO4, FDA and A2P 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FNC OCA].
+FNC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=FDA:'>FDA</scene> and <scene name='pdbligand=A2P:'>A2P</scene> 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FNC OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Spinacia oleracea]]
-[[Category: Bruns, C.M.]]
+[[Category: Bruns, C M.]]
-[[Category: Karplus, P.A.]]
+[[Category: Karplus, P A.]]
 [[Category: A2P]]
 [[Category: FDA]]
@@ Line 22: / Line 22: @@
 [[Category: oxidoreductase (nadp+(a)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:03:44 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:32 2008''