4fxc

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(New page: 200px<br /><applet load="4fxc" size="450" color="white" frame="true" align="right" spinBox="true" caption="4fxc, resolution 2.5&Aring;" /> '''TERTIARY STRUCTURE OF...)
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[[Image:4fxc.jpg|left|200px]]<br /><applet load="4fxc" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="4fxc, resolution 2.5&Aring;" />
 
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'''TERTIARY STRUCTURE OF [2FE-2S] FERREDOXIN FROM SPIRULINA PLATENSIS REFINED AT 2.5 ANGSTROMS RESOLUTION: STRUCTURAL COMPARISONS OF PLANT-TYPE FERREDOXINS AND AN ELECTROSTATIC POTENTIAL ANALYSIS'''<br />
 
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==Overview==
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==TERTIARY STRUCTURE OF [2FE-2S] FERREDOXIN FROM SPIRULINA PLATENSIS REFINED AT 2.5 ANGSTROMS RESOLUTION: STRUCTURAL COMPARISONS OF PLANT-TYPE FERREDOXINS AND AN ELECTROSTATIC POTENTIAL ANALYSIS==
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The structure of plant-type [2Fe-2S] ferredoxin isolated from Spirulina, platensis has been refined using diffraction data to 2.5 A resolution by, alternate cycles of simulated annealing and manual revision of the model., The final R factor is 19.9% for 2,912 reflections with F &gt; 2 sigma F, between 8.0 and 2.5 A resolution. S. platensis ferredoxin, like other, plant-type [2Fe-2S] ferredoxins, has a major alpha-helix flanking a sheet, consisting of four beta strands. The present refinement revises the, conformation of residues 56-71, in which a one-turn helix was identified., Superposition of the Spirulina ferredoxin structure on the structures of, other ferredoxins that have been well refined showed structural, perturbation at a few residues on the amino and carboxyl termini and the, turn between the first and second beta-strands. The root-mean-square, deviations of the corresponding C alpha atoms of the pairs of ferredoxins, range from 0.90 to 1.17 A for all the residues, but from 0.64 to 0.70 A if, the few perturbed residues are excluded. Therefore, it may be concluded, that the main-chain foldings of all the plant-type [2Fe-2S] ferredoxins, are essentially the same. Electrostatic potential analysis showed that the, molecular surface around the cluster is negatively charged, whereas that, of the beta-sheet of the other side is positively charged. The interaction, between ferredoxin and ferredoxin-NADP+ reductase is discussed on the, basis of the charge distributions of these molecules and biochemical data.
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<StructureSection load='4fxc' size='340' side='right'caption='[[4fxc]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4fxc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arthrospira_platensis Arthrospira platensis]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3fxc 3fxc] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1fxc 1fxc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FXC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FXC FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fxc OCA], [https://pdbe.org/4fxc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fxc RCSB], [https://www.ebi.ac.uk/pdbsum/4fxc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fxc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FER_ARTPT FER_ARTPT] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fx/4fxc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=4fxc ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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4FXC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrospira_platensis Arthrospira platensis] with FES as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entries 3FXC and 1FXC. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4FXC OCA].
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*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Tertiary structure of [2Fe-2S] ferredoxin from Spirulina platensis refined at 2.5 A resolution: structural comparisons of plant-type ferredoxins and an electrostatic potential analysis., Fukuyama K, Ueki N, Nakamura H, Tsukihara T, Matsubara H, J Biochem (Tokyo). 1995 May;117(5):1017-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8586613 8586613]
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[[Category: Arthrospira platensis]]
[[Category: Arthrospira platensis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Fukuyama, K.]]
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[[Category: Fukuyama K]]
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[[Category: Tsukihara, T.]]
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[[Category: Tsukihara T]]
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[[Category: FES]]
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[[Category: electron transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:36:08 2007''
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Current revision

TERTIARY STRUCTURE OF [2FE-2S] FERREDOXIN FROM SPIRULINA PLATENSIS REFINED AT 2.5 ANGSTROMS RESOLUTION: STRUCTURAL COMPARISONS OF PLANT-TYPE FERREDOXINS AND AN ELECTROSTATIC POTENTIAL ANALYSIS

PDB ID 4fxc

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