1fnc: Difference between revisions

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New page: left|200px<br /><applet load="1fnc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fnc, resolution 2.0Å" /> '''REFINED CRYSTAL STRUC...
 
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[[Image:1fnc.gif|left|200px]]<br /><applet load="1fnc" size="450" 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==
==REFINED CRYSTAL STRUCTURE OF SPINACH FERREDOXIN REDUCTASE AT 1.7 ANGSTROMS RESOLUTION: OXIDIZED, REDUCED, AND 2'-PHOSPHO-5'-AMP BOUND STATES==
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.
<StructureSection load='1fnc' size='340' side='right'caption='[[1fnc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1fnc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FNC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FNC FirstGlance]. <br>
1FNC 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].  
</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&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2P:ADENOSINE-2-5-DIPHOSPHATE'>A2P</scene>, <scene name='pdbligand=FDA:DIHYDROFLAVINE-ADENINE+DINUCLEOTIDE'>FDA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fnc OCA], [https://pdbe.org/1fnc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fnc RCSB], [https://www.ebi.ac.uk/pdbsum/1fnc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fnc ProSAT]</span></td></tr>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7897656 7897656]
</table>
[[Category: Ferredoxin--NADP(+) reductase]]
== Function ==
[[Category: Single protein]]
[https://www.uniprot.org/uniprot/FENR_SPIOL FENR_SPIOL] May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power.
== 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/fn/1fnc_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=1fnc ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Spinacia oleracea]]
[[Category: Spinacia oleracea]]
[[Category: Bruns, C.M.]]
[[Category: Bruns CM]]
[[Category: Karplus, P.A.]]
[[Category: Karplus PA]]
[[Category: A2P]]
[[Category: FDA]]
[[Category: SO4]]
[[Category: ferredoxin(a))]]
[[Category: oxidoreductase (nadp+(a)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:03:44 2007''

Latest revision as of 10:16, 7 February 2024

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

Structural highlights

1fnc is a 1 chain structure with sequence from Spinacia oleracea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FENR_SPIOL May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1fnc, resolution 2.00Å

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