An Engineered Pathway for the Formation of Protein Disulfide Bonds

Science

Volumn 303, Issue 5661, 2004, Pages 1185-1189

  Masip, Lluis ^a   Pan, Jonathan L ^b   Haldar, Suranjana ^b   Penner Hahn, James E ^b   DeLisa, Matthew P ^a   Georgiou, George ^a   Bardwell, James C A ^b   Collet, Jean François ^b  

^a The University of Texas at Austin   (United States)

^b UNIVERSITY OF MICHIGAN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CELLS; CHEMICAL BONDS; ESCHERICHIA COLI; MUTAGENESIS; OXIDATION;

COFACTORS; DISULFIDE BONDS;

PROTEINS;

BACTERIAL PROTEIN; CYSTEINE; DIMER; DISULFIDE; DISULFIDE REDUCTASE; DSBA PROTEIN; DSBB PROTEIN; DSBB PROTEIN, BACTERIA; HIRUDIN; IRON; MEMBRANE PROTEIN; MONOMER; MUTANT PROTEIN; OXIDOREDUCTASE; OXYGEN; PROTEIN; PROTEIN DISULFIDE ISOMERASE; SULFIDE; THIOL DERIVATIVE; THIOREDOXIN; UNCLASSIFIED DRUG;

PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CELL MEMBRANE; CHEMISTRY; CYTOPLASM; DIMERIZATION; DIRECTED MOLECULAR EVOLUTION; DISULFIDE BOND; ESCHERICHIA COLI; EVOLUTION; GENETICS; METABOLISM; MOVEMENT (PHYSIOLOGY); MUTATION; NONHUMAN; OXIDATION; OXIDATION REDUCTION REACTION; PHYSIOLOGY; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN MOTIF;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; CELL MEMBRANE; CYSTEINE; CYTOPLASM; DIMERIZATION; DIRECTED MOLECULAR EVOLUTION; DISULFIDES; ESCHERICHIA COLI; HIRUDINS; IRON; MEMBRANE PROTEINS; MOVEMENT; MUTATION; OXIDATION-REDUCTION; OXYGEN; PROTEIN DISULFIDE-ISOMERASE; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEINS; SULFIDES; THIOREDOXIN;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 1242284596     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1092612     Document Type: Article

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23. We thank U. Jakob, P. Kiley, and H. Beinert for many helpful discussions; D. Ballou for help on spectrophotometric measurements; H. Beinert for doing the sulfide assays; T. Huston for performing the ICP-high resolution mass spectroscopy analyses; and T. Palmer and F. Sargent for reading the manuscript. X-ray absorption spectroscopy data were measured at the National Synchrotron Light Source, which is supported by the U.S. Department of Energy (contract no. DE-AC02-98CH10886), at line X9-B, which is supported by the NIH National Center for Research Resources (grant no. P41-RR01633). This work was supported by the Foundation for Research; NSF grant no. BES-220393 (G.G.); and NIH grant nos. GM-55090 (G.G.), GM-57039 and GM-64662 (J.C.A.B.), and GM-38047 (J.E.P.H.). J.F.C. is Charge de Recherches of the Belgian Fonds National de la Recherche Scientifique.