3kap: Difference between revisions
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==Flavodoxin from Desulfovibrio desulfuricans ATCC 27774 (oxidized form)== | ==Flavodoxin from Desulfovibrio desulfuricans ATCC 27774 (oxidized form)== | ||
<StructureSection load='3kap' size='340' side='right' caption='[[3kap]], [[Resolution|resolution]] 2.05Å' scene=''> | <StructureSection load='3kap' size='340' side='right'caption='[[3kap]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3kap]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans_subsp._desulfuricans_str._atcc_27774 Desulfovibrio desulfuricans subsp. desulfuricans str. atcc 27774]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KAP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KAP FirstGlance]. <br> | <table><tr><td colspan='2'>[[3kap]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans_subsp._desulfuricans_str._atcc_27774 Desulfovibrio desulfuricans subsp. desulfuricans str. atcc 27774]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KAP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KAP 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/ka/3kap_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ka/3kap_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 3kap" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3kap" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Flavodoxin 3D structures|Flavodoxin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Desulfovibrio desulfuricans subsp. desulfuricans str. atcc 27774]] | [[Category: Desulfovibrio desulfuricans subsp. desulfuricans str. atcc 27774]] | ||
[[Category: Large Structures]] | |||
[[Category: Caldeira, J]] | [[Category: Caldeira, J]] | ||
[[Category: LeGall, J]] | [[Category: LeGall, J]] | ||
Revision as of 10:19, 7 August 2019
Flavodoxin from Desulfovibrio desulfuricans ATCC 27774 (oxidized form)Flavodoxin from Desulfovibrio desulfuricans ATCC 27774 (oxidized form)
Structural highlights
Function[FLAW_DESDA] Low-potential electron donor to a number of redox enzymes. 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 PubMedThe crystal structures of the flavodoxin from Desulfovibrio desulfuricans ATCC 27774 have been determined and refined for both oxidized and semi-reduced forms to final crystallographic R-factors of 17.9% (0.8-0.205-nm resolution) and 19.4% (0.8-0.215-nm resolution) respectively. Native flavodoxin crystals were grown from ammonium sulfate with cell constants a = b = 9.59 nm, c=3.37nm (oxidized crystals) and they belong to space group P3(2)21. Semireduced crystals showed some changes in cell dimensions: a = b = 9.51 nm, c=3.35 nm. The three-dimensional structures are similar to other known flavodoxins and deviations are found essentially in the isoalloxazine ring environment. Conformational changes are observed between both redox states and a flip of the Gly61-Met62 peptide bond occurs upon one-electron reduction of the FMN group. These changes influence the redox potential of the oxidized/semiquinone couple. Modulation of the redox potentials is known to be related to the association constant of the FMN group to the protein. The flavodoxin from D. desulfuricans now studied has a large span between E2 (oxidized --> semiquinone) and E1 (semiquinone --> hydroquinone) redox potentials, both these values being substantially more positive within known flavodoxins. A comparison of their FMN environment was made in both oxidation states in order to correlate functional and structural differences. Crystal structure of flavodoxin from Desulfovibrio desulfuricans ATCC 27774 in two oxidation states.,Romero A, Caldeira J, Legall J, Moura I, Moura JJ, Romao MJ Eur J Biochem. 1996 Jul 1;239(1):190-6. PMID:8706707[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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