1xwc: Difference between revisions
New page: left|200px<br /><applet load="1xwc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xwc, resolution 2.3Å" /> '''Drosophila thioredoxi... |
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[[Image:1xwc.gif|left|200px]]<br /><applet load="1xwc" size=" | [[Image:1xwc.gif|left|200px]]<br /><applet load="1xwc" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''Drosophila thioredoxin, reduced, P6522'''<br /> | '''Drosophila thioredoxin, reduced, P6522'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1XWC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http:// | 1XWC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XWC OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: x-ray crystal structure]] | [[Category: x-ray crystal structure]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:46:22 2008'' | ||
Revision as of 15:46, 23 January 2008
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Drosophila thioredoxin, reduced, P6522
OverviewOverview
Thioredoxins (Trx) participate in essential antioxidant and, redox-regulatory processes via a pair of conserved cysteine residues. In, dipteran insects like Drosophila and Anopheles, which lack a genuine, glutathione reductase (GR), thioredoxins fuel the glutathione system with, reducing equivalents. Thus, characterizing Trxs from these organisms, contributes to our understanding of redox control in GR-free systems and, provides information on novel targets for insect control. Cytosolic Trx of, Drosophila melanogaster (DmTrx) is the first thioredoxin that was, crystallized for X-ray diffraction analysis in the reduced and in the, oxidized form. Comparison of the resulting structures shows rearrangements, in the active-site regions. Formation of the C32-C35 disulfide bridge, leads to a rotation of the side-chain of C32 away from C35 in the reduced, form. This is similar to the situation in human Trx and Trx m from spinach, chloroplasts but differs from Escherichia coli Trx, where it is C35 that, moves upon change of the redox state. In all four crystal forms that were, analysed, DmTrx molecules are engaged in a non-covalent dimer interaction., However, as demonstrated by gel-filtration analyses, DmTrx does not, dimerize under quasi in vivo conditions and there is no redox control of a, putative monomer/dimer equilibrium. The dimer dissociation constants K(d), were found to be 2.2mM for reduced DmTrx and above 10mM for oxidized DmTrx, as well as for the protein in the presence of reduced glutathione. In, human Trx, oxidative dimerization has been demonstrated in vitro., Therefore, this finding may indicate a difference in redox control of, GR-free and GR-containing organisms.
About this StructureAbout this Structure
1XWC is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
ReferenceReference
Comparative structural analysis of oxidized and reduced thioredoxin from Drosophila melanogaster., Wahl MC, Irmler A, Hecker B, Schirmer RH, Becker K, J Mol Biol. 2005 Feb 4;345(5):1119-30. Epub 2004 Dec 16. PMID:15644209
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