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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 motif

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Journal of Structural and Functional Genomics

Abstract

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.

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Abbreviations

NESG:

Northeast Structural Genomics Consortium

NMR:

Nuclear magnetic resonance

NSLF:

National synchrotron light source

PDB:

Protein data bank

RDC:

Residual dipolar coupling

PSVS:

Protein structure validation suite

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Acknowledgements

This work was supported by the National Institutes of Health (U54 GM074958–01) and the National Science Foundation (MCB 0416899 to T.S.). We thank Kellie Cunningham, Chi Kent Ho, Haleema Janjua, Li-Chung Ma, and Li Zhao (Rutgers University) for help preparing the protein samples.

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Authors and Affiliations

  1. Department of Chemistry, Northeast Structural Genomics Consortium, The State University of New York at Buffalo, Buffalo, NY, 14260, USA

    David Parish, Goahua Liu, Kiran Kumar Singarapu & Thomas Szyperski

  2. Department of Biological Sciences, Northeast Structural Genomics Consortium, Columbia University, New York, NY, 10027, USA

    Jordi Benach, Min Su & John Hunt

  3. The Center for Advanced Biotechnology and Medicine, Department of Molecular Biology and Biochemistry, Northeast Structural Genomics Consortium, Rutgers University and Robert Wood Johnson Medical School, Piscataway, NJ, 08854, USA

    Rong Xiao, Thomas Acton & Gaetano T. Montelione

  4. Complex Carbohydrate Research Center and Department of Chemistry, University of Georgia, Athens, GA, 30602-4712, USA

    Sonal Bansal & James H. Prestegard

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  1. David Parish
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Correspondence to Thomas Szyperski.

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Parish, D., Benach, J., Liu, G. et al. 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 motif. J Struct Funct Genomics 9, 41–49 (2008). https://doi.org/10.1007/s10969-008-9050-y

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