|Journal of Structural and Functional Genomics (2008) 9:41-9|
|Northeast Structural Genomics Consortium|
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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 Escherichia coli was determined by NMR. ...
The two proteins belong to Pfam (Finn et al. 34:D247-D251, 2006) 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.
|metabolism chemistry genetics |
|Catalytic Domain Amino Acid Sequence Models, Molecular Molecular Sequence Data Escherichia coli Escherichia coli Proteins Sequence Alignment Protein Conformation Sequence Homology, Amino Acid Bacterial Proteins Salmonella typhimurium Magnetic Resonance Spectroscopy Thioredoxins Molecular Chaperones |
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