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

David Parish, Jordi Benach, Goahua Liu, Kiran Kumar Singarapu, Rong Xiao, Thomas Acton, Min Su, Sonal Bansal, James H. Prestegard, John Hunt, Gaetano Montelione, Thomas Szyperski

Research output: Contribution to journalArticle

10 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)41-49
Number of pages9
JournalJournal of Structural and Functional Genomics
Volume9
Issue number1-4
DOIs
StatePublished - Dec 1 2008

Fingerprint

Thioredoxins
Salmonella
Salmonella typhimurium
Escherichia coli
Catalytic Domain
Proteins
Protein Sorting Signals
Arginine
Genes
Nuclear magnetic resonance
Genome
X ray crystallography
X Ray Crystallography

All Science Journal Classification (ASJC) codes

  • Genetics
  • Structural Biology
  • Biochemistry

Keywords

  • Chaperones
  • GFT NMR
  • HYAE_ECOLI
  • Q8ZP25_SALTY
  • Structural genomics
  • Thioredoxin

Cite this

Parish, David ; Benach, Jordi ; Liu, Goahua ; Singarapu, Kiran Kumar ; Xiao, Rong ; Acton, Thomas ; Su, Min ; Bansal, Sonal ; Prestegard, James H. ; Hunt, John ; Montelione, Gaetano ; Szyperski, Thomas. / 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. In: Journal of Structural and Functional Genomics. 2008 ; Vol. 9, No. 1-4. pp. 41-49.
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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. / Parish, David; Benach, Jordi; Liu, Goahua; Singarapu, Kiran Kumar; Xiao, Rong; Acton, Thomas; Su, Min; Bansal, Sonal; Prestegard, James H.; Hunt, John; Montelione, Gaetano; Szyperski, Thomas.

In: Journal of Structural and Functional Genomics, Vol. 9, No. 1-4, 01.12.2008, p. 41-49.

Research output: Contribution to journalArticle

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AU - Acton, Thomas

AU - Su, Min

AU - Bansal, Sonal

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AU - Szyperski, Thomas

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