Protein chaperones Q8ZP25_SALTY from Salmonella typhimurium and HYAE_ECOLI from Escherichia coli exhibit thioredoxin-like structures despite lack of canonical thioredoxin active site sequence motive
The structure of the 142-residue protein Q8ZP25_SALTY encoded in the genome of Salmonella typhimurium LT2 was determined independently by NMR and X-ray crystallography, and the structure of the 140-residue protein HYAE_ECOLI encoded in the genome of Eschericia coli was determined by NMR. The two pro...
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Published in | Journal of structural and functional genomics Vol. 9; no. 1-4; pp. 41 - 49 |
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Main Authors | , , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
26.11.2008
|
Online Access | Get full text |
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Summary: | The structure of the 142-residue protein Q8ZP25_SALTY encoded in the genome of
Salmonella typhimurium
LT2 was determined independently by NMR and X-ray crystallography, and the structure of the 140-residue protein HYAE_ECOLI encoded in the genome of
Eschericia coli
was determined by NMR. The two proteins belong to Pfam [
1
] PF07449, which currently comprises 50 members, and belongs itself to the ‘thioredoxin-like clan’. However, protein HYAE_ECOLI and the other proteins of Pfam PF07449 do not contain the canonical Cys-X-X-Cys active site sequence motif of thioredoxin. Protein HYAE_ECOLI was previously classified as a [NiFe] hydrogenase-1 specific chaperone interacting with the twin-arginine translocation (Tat) signal peptide. The structures presented here exhibit the expected thioredoxin-like fold and support the view that members of Pfam family PF07449 specifically interact with Tat signal peptides. |
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ISSN: | 1345-711X 1570-0267 |
DOI: | 10.1007/s10969-008-9050-y |