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3fx2

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COMPARISON OF THE CRYSTAL STRUCTURES OF A FLAVODOXIN IN ITS THREE OXIDATION STATES AT CRYOGENIC TEMPERATURES

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Retrieved from "http://52.214.119.220/wiki/index.php/3fx2"

Categories: Desulfovibrio vulgaris | Large Structures | Watenpaugh KD | Watt W

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-[[Image:3fx2.jpg|left|200px]]<br /><applet load="3fx2" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="3fx2, resolution 1.9&Aring;" />
-'''COMPARISON OF THE CRYSTAL STRUCTURES OF A FLAVODOXIN IN ITS THREE OXIDATION STATES AT CRYOGENIC TEMPERATURES'''<br />
-==Overview==
+==COMPARISON OF THE CRYSTAL STRUCTURES OF A FLAVODOXIN IN ITS THREE OXIDATION STATES AT CRYOGENIC TEMPERATURES==
-The focus of this study has been to determine the conformation of the, holoprotein of recombinant flavodoxin from Desulfovibrio vulgaris with the, FMN in each of its three oxidation states. The structures of the oxidized, state of the wild-type flavodoxin at 2.0 A from D. vulgaris was used as a, starting model for refinement. Diffraction experiments were conducted at, low temperature (-150 degrees C) in order to maintain the oxidation state, of interest throughout the intensity data collection. yellow bipyramids by, the standard hanging-drop method from 3.2 M-ammonium sulfate in 0.1, M-Tris-HCl buffer at pH 7.0 with protein concentrations ranging from 0.7%, to 0.9%. The reduced states of the crystals were achieved through the, addition of sodium dithionite at pH 7.0 for the semiquinone (semi-reduced), and at pH 9.0 for the hydroquinone (fully reduced). Data sets consisting, of one at room temperature (oxidized state) and three at low temperature, (each oxidation state) were collected on a Nicolet P3F/Xentronics area, detector X-ray diffractometer system. The four structures, hydroquinone at, 2.25 A resolution and all others at 1.9 A resolution, were refined by the, restrained parameter least-squares program PROLSQ. The final, crystallographic R-values converged to 0.21 (hydroquinone), 0.20, (semiquinone), 0.20 (oxidized, low temperature), and 0.17 (oxidized, room, temperature). The reduced states of flavodoxin show a different, conformation of the protein polypeptide chain (Asp61-Gly62) in the, vicinity of NH(5) of the isoalloxazine group relative to the oxidized, state. However, there are only slight conformational differences between, the semiquinone and hydroquinone states. In this report, structural, comparisons of the three are made, with particular emphasis on the, features that might be related to the difference in temperature of the, diffraction data collections and differences in the oxidation state of the, FMN.
+<StructureSection load='3fx2' size='340' side='right'caption='[[3fx2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3fx2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FX2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FX2 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fx2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fx2 OCA], [https://pdbe.org/3fx2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fx2 RCSB], [https://www.ebi.ac.uk/pdbsum/3fx2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fx2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FLAV_DESVH FLAV_DESVH] Low-potential electron donor to a number of redox enzymes.
+== 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/fx/3fx2_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=3fx2 ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-FX2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] with FMN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3FX2 OCA].
+*[[Flavodoxin 3D structures|Flavodoxin 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Comparison of the crystal structures of a flavodoxin in its three oxidation states at cryogenic temperatures., Watt W, Tulinsky A, Swenson RP, Watenpaugh KD, J Mol Biol. 1991 Mar 5;218(1):195-208. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2002503 2002503]
 [[Category: Desulfovibrio vulgaris]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Watenpaugh, K.D.]]
+[[Category: Watenpaugh KD]]
-[[Category: Watt, W.]]
+[[Category: Watt W]]
-[[Category: FMN]]
-[[Category: electron transport]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:43:54 2007''

3fx2

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COMPARISON OF THE CRYSTAL STRUCTURES OF A FLAVODOXIN IN ITS THREE OXIDATION STATES AT CRYOGENIC TEMPERATURES

Structural highlights

Function

Evolutionary Conservation

See Also

Contents

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