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TitleProtein 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.
Journal, issue, pagesJ. STRUCT. FUNCT. GENOM., Vol. 9, Page 41-49, Year 2008
Publish dateJun 23, 2006 (structure data deposition date)
AuthorsParish, D. / Benach, J. / Liu, G. / Singarapu, K.K. / Xiao, R. / Acton, T. / Su, M. / Bansal, S. / Prestegard, J.H. / Hunt, J. ...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.
External linksJ. STRUCT. FUNCT. GENOM. / PubMed:19039680
MethodsNMR (solution)
Structure data

PDB-2hfd:
NMR structure of protein Hydrogenase-1 operon protein hyaE from Escherichia coli: Northeast Structural Genomics Consortium Target ER415
Method: SOLUTION NMR

PDB-2jzt:
Solution NMR structure of Q8ZP25_SALTY from Salmonella typhimurium. Northeast Structural Genomics Consortium target StR70
Method: SOLUTION NMR

Source
  • escherichia coli (E. coli)
  • salmonella typhimurium lt2 (bacteria)
KeywordsSTRUCTURAL GENOMICS / UNKNOWN FUNCTION / PROTEIN STRUCTURE / NESGC / ALFA-BETA / PSI-2 / Protein Structure Initiative / Northeast Structural Genomics Consortium / ISOMERASE / NESG / StR70 / Putative [NiFe] hydrogenase assembly / Chaperone

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