1fdr: Difference between revisions

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-[[Image:1fdr.gif|left|200px]]<br /><applet load="1fdr" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1fdr, resolution 1.70&Aring;" />
-'''FLAVODOXIN REDUCTASE FROM E. COLI'''<br />
-==Overview==
+==FLAVODOXIN REDUCTASE FROM E. COLI==
-Flavodoxin reductase from Escherichia coli is an FAD-containing oxidoreductase that transports electrons between flavodoxin or ferredoxin and NADPH. Together with flavodoxin, the enzyme is involved in the reductive activation of three E. coli enzymes: cobalamin-dependent methionine synthase, pyruvate formate lyase and anaerobic ribonucleotide reductase. An additional function for the oxidoreductase appears to be to protect the bacteria against oxygen radicals. The three-dimensional structure of flavodoxin reductase has been solved by multiple isomorphous replacement, and has been refined at 1.7 A to an R-value of 18.4% and Rfree 24.8%. The monomeric molecule contains one beta-sandwich FAD domain and an alpha/beta NADP domain. The overall structure is similar to other reductases of the NADP-ferredoxin reductase family in spite of the low sequence similarities within the family. Flavodoxin reductase lacks the loop which is involved in the binding of the adenosine moiety of FAD in other FAD binding enzymes of the superfamily but is missing in the FMN binding phthalate dioxygenase reductase. Instead of this loop, the adenine interacts with an extra tryptophan at the C terminus. The FAD in flavodoxin reductase has an unusual bent conformation with a hydrogen bond between the adenine and the isoalloxazine. This is probably the cause of the unusual spectrum of the enzyme. There is a pronounced cleft close to the isoalloxazine that appears to be well suited for binding of flavodoxin/ferredoxin. Two extra short strands of the NADP-binding domain probably act as an anchor point for the binding of flavodoxin.
+<StructureSection load='1fdr' size='340' side='right'caption='[[1fdr]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+== Structural highlights ==
-==About this Structure==
+<table><tr><td colspan='2'>[[1fdr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FDR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FDR FirstGlance]. <br>
-FDR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1FDR 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]] 1.7&#8491;</td></tr>
+<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>
-==Reference==
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fdr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fdr OCA], [https://pdbe.org/1fdr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fdr RCSB], [https://www.ebi.ac.uk/pdbsum/1fdr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fdr ProSAT]</span></td></tr>
-The three-dimensional structure of flavodoxin reductase from Escherichia coli at 1.7 A resolution., Ingelman M, Bianchi V, Eklund H, J Mol Biol. 1997 Apr 25;268(1):147-57. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9149148 9149148]
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FENR_ECOLI FENR_ECOLI] Transports electrons between flavodoxin or ferredoxin and NADPH. Involved in the reductive activation of cobalamin-independent methionine synthase, pyruvate formate lyase and anaerobic ribonucleotide reductase. Also protects against superoxide radicals due to methyl viologen in the presence of oxygen.
+== 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/fd/1fdr_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=1fdr ConSurf].
+<div style="clear:both"></div>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Ferredoxin--NADP(+) reductase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Bianchi V]]
-[[Category: Bianchi, V.]]
+[[Category: Eklund H]]
-[[Category: Eklund, H.]]
+[[Category: Ingelman M]]
-[[Category: Ingelman, M.]]
-[[Category: FAD]]
-[[Category: ferredoxin reductase]]
-[[Category: flavin]]
-[[Category: flavodoxin reductase]]
-[[Category: flavoprotein]]
-[[Category: oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:37:37 2008''