1awd: Difference between revisions
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==FERREDOXIN [2FE-2S] OXIDIZED FORM FROM CHLORELLA FUSCA== | ==FERREDOXIN [2FE-2S] OXIDIZED FORM FROM CHLORELLA FUSCA== | ||
<StructureSection load='1awd' size='340' side='right' caption='[[1awd]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='1awd' size='340' side='right'caption='[[1awd]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1awd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/'chlorella'_fusca 'chlorella' fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AWD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AWD FirstGlance]. <br> | <table><tr><td colspan='2'>[[1awd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/'chlorella'_fusca 'chlorella' fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AWD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AWD FirstGlance]. <br> | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aw/1awd_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aw/1awd_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1awd" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1awd" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Chlorella fusca]] | [[Category: Chlorella fusca]] | ||
[[Category: Large Structures]] | |||
[[Category: Sheldrick, G M]] | [[Category: Sheldrick, G M]] | ||
[[Category: Electron transfer]] | [[Category: Electron transfer]] | ||
Revision as of 19:19, 28 August 2019
FERREDOXIN [2FE-2S] OXIDIZED FORM FROM CHLORELLA FUSCAFERREDOXIN [2FE-2S] OXIDIZED FORM FROM CHLORELLA FUSCA
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBACKGROUND: [2Fe-2S] ferredoxins, also called plant-type ferredoxins, are low-potential redox proteins that are widely distributed in biological systems. In photosynthesis, the plant-type ferredoxins function as the central molecule for distributing electrons from the photolysis of water to a number of ferredox-independent enzymes, as well as to cyclic photophosphorylation electron transfer. This paper reports only the second structure of a [2Fe-2S] ferredoxin from a eukaryotic organism in its native form. RESULTS: Ferredoxin from the green algae Chlorella fusca has been purified, characterised, crystallised and its structure determined to 1.4 A resolution - the highest resolution structure published to date for a plant-type ferredoxin. The structure has the general features of the plant-type ferredoxins already described, with conformational differences corresponding to regions of higher mobility. Immunological data indicate that a serine residue within the protein is partially phosphorylated. A slightly electropositive shift in the measured redox potential value, -325 mV, is observed in comparison with other ferredoxins. CONCLUSIONS: This high-resolution structure provides a detailed picture of the hydrogen-bonding pattern around the [2Fe-2S] cluster of a plant-type ferredoxin; for the first time, it was possible to obtain reliable error estimates for the geometrical parameters. The presence of phosphoserine in the protein indicates a possible mechanism for the regulation of the distribution of reducing power from the photosynthetic electron-transfer chain. Crystal structure determination at 1.4 A resolution of ferredoxin from the green alga Chlorella fusca.,Bes MT, Parisini E, Inda LA, Saraiva LM, Peleato ML, Sheldrick GM Structure. 1999 Oct 15;7(10):1201-11. PMID:10545324[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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