1fnc: Difference between revisions

Revision as of 03:36, 1 July 2008

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File:1fnc.png

Template:STRUCTURE 1fnc

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

Template:ABSTRACT PUBMED 7897656

About this StructureAbout this Structure

1FNC is a Single protein structure of sequence from Spinacia oleracea. 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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OCA

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-[[Image:1fnc.gif|left|200px]]
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 {{STRUCTURE_1fnc|  PDB=1fnc  |  SCENE=  }}
-'''REFINED CRYSTAL STRUCTURE OF SPINACH FERREDOXIN REDUCTASE AT 1.7 ANGSTROMS RESOLUTION: OXIDIZED, REDUCED, AND 2'-PHOSPHO-5'-AMP BOUND STATES'''
+===REFINED CRYSTAL STRUCTURE OF SPINACH FERREDOXIN REDUCTASE AT 1.7 ANGSTROMS RESOLUTION: OXIDIZED, REDUCED, AND 2'-PHOSPHO-5'-AMP BOUND STATES===
-==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 line below this paragraph, {{ABSTRACT_PUBMED_7897656}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7897656 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_7897656}}
 ==About this Structure==
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 [[Category: Bruns, C M.]]
 [[Category: Karplus, P A.]]
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