2HFD

NMR structure of protein Hydrogenase-1 operon protein hyaE from Escherichia coli: Northeast Structural Genomics Consortium Target ER415

Summary for 2HFD

• Entry DOI: 10.2210/pdb2hfd/pdb
• NMR Information: BMRB: 7256
• Descriptor: Hydrogenase-1 operon protein hyaE (1 entity in total)
• Functional Keywords: protein structure, nesgc, alfa-beta, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, unknown function
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 15972.87

Authors

Singarapu, K.K.,Liu, G.,Eletsky, A.,Parish, D.,Atreya, H.S.,Xu, D.,Janjua, H.,Cunningham, K.,Ma, L.C.,Xiao, R.,Liu, J.,Baran, M.,Swapna, G.V.T.,Acton, T.,Rost, B.,Montelione, G.T.,Szyperski, T.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2006-06-23, release date: 2006-08-22, Last modification date: 2024-05-01)

Primary citation

Parish, D.,Benach, J.,Liu, G.,Singarapu, K.K.,Xiao, R.,Acton, T.,Su, M.,Bansal, S.,Prestegard, J.H.,Hunt, J.,Montelione, G.T.,Szyperski, T.
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.GENOM., 9:41-49, 2008

PubMed 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.

PubMed: 19039680
DOI: 10.1007/s10969-008-9050-y

Experimental method

SOLUTION NMR