1zcp

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[[Image:1zcp.gif|left|200px]]
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{{Structure
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|GENE= trxA, fipA, tsnC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zcp OCA], [http://www.ebi.ac.uk/pdbsum/1zcp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zcp RCSB]</span>
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'''Crystal Structure of a catalytic site mutant E. coli TrxA (CACA)'''
'''Crystal Structure of a catalytic site mutant E. coli TrxA (CACA)'''
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[[Category: Peisach, D.]]
[[Category: Peisach, D.]]
[[Category: Xu, Z.]]
[[Category: Xu, Z.]]
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[[Category: electron transport]]
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[[Category: Electron transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:28:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:34:04 2008''
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Revision as of 14:28, 3 May 2008

Template:STRUCTURE 1zcp

Crystal Structure of a catalytic site mutant E. coli TrxA (CACA)


Overview

Escherichia coli thioredoxin is a small monomeric protein that reduces disulfide bonds in cytoplasmic proteins. Two cysteine residues present in a conserved CGPC motif are essential for this activity. Recently, we identified mutations of this motif that changed thioredoxin into a homodimer bridged by a [2Fe-2S] iron-sulfur cluster. When exported to the periplasm, these thioredoxin mutants could restore disulfide bond formation in strains lacking the entire periplasmic oxidative pathway. Essential for the assembly of the iron-sulfur was an additional cysteine that replaced the proline at position three of the CGPC motif. We solved the crystalline structure at 2.3 Angstroms for one of these variants, TrxA(CACA). The mutant protein crystallized as a dimer in which the iron-sulfur cluster is replaced by two intermolecular disulfide bonds. The catalytic site, which forms the dimer interface, crystallized in two different conformations. In one of them, the replacement of the CGPC motif by CACA has a dramatic effect on the structure and causes the unraveling of an extended alpha-helix. In both conformations, the second cysteine residue of the CACA motif is surface-exposed, which contrasts with wildtype thioredoxin where the second cysteine of the CXXC motif is buried. This exposure of a pair of vicinal cysteine residues apparently allows thioredoxin to acquire an iron-sulfur cofactor at its active site, and thus a new activity and mechanism of action.

About this Structure

1ZCP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The crystal structure of TrxA(CACA): Insights into the formation of a [2Fe-2S] iron-sulfur cluster in an Escherichia coli thioredoxin mutant., Collet JF, Peisach D, Bardwell JC, Xu Z, Protein Sci. 2005 Jul;14(7):1863-9. PMID:15987909 Page seeded by OCA on Sat May 3 17:28:09 2008

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