title: 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.
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.
authors.affiliation: Department of Chemistry, Northeast Structural Genomics Consortium, The State University of New York at Buffalo, Buffalo, NY 14260, USA.
authors.forename: David
authors.initials: D
authors.lastname: Parish
authors.forename: Jordi
authors.initials: J
authors.lastname: Benach
authors.forename: Goahua
authors.initials: G
authors.lastname: Liu
authors.forename: Kiran Kumar
authors.initials: KK
authors.lastname: Singarapu
authors.forename: Rong
authors.initials: R
authors.lastname: Xiao
authors.forename: Thomas
authors.initials: T
authors.lastname: Acton
authors.forename: Min
authors.initials: M
authors.lastname: Su
authors.forename: Sonal
authors.initials: S
authors.lastname: Bansal
authors.forename: James H
authors.initials: JH
authors.lastname: Prestegard
authors.forename: John
authors.initials: J
authors.lastname: Hunt
authors.forename: Gaetano T
authors.initials: GT
authors.lastname: Montelione
authors.forename: Thomas
authors.initials: T
authors.lastname: Szyperski
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D020134:Catalytic Domain; D004926:Escherichia coli / Q000235:genetics*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012486:Salmonella typhimurium / Q000235:genetics* / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013879:Thioredoxins / Q000235:genetics*
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D018832:Molecular Chaperones; D013879:Thioredoxins