Nucleotide sequence of the thioredoxin gene from <i>Escherichia coli</i>

Höög, Jan‐Olov; Bahr‐Lindström, Hedvig von; Josephson, Staffan; Wallace, B J; Kushner, Sidney R.; Jörnvall, Hans; Holmgren, Arne

doi:10.1007/bf01116889

Cited by 39 publications

(1 citation statement)

References 26 publications

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“…Fusion protein structures were identified by using the Basic Local Alignment Search Tool (BLAST) server to query the PDB with the amino acid sequences of E. coli MBP, E. coli TRX, and Schistosoma japonicum GST . The matches were then inspected manually to identify the fusion proteins.…”

Section: Methodsmentioning

confidence: 99%

Crystal structures of MBP fusion proteins

Waugh

2016

Protein Science

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Although chaperone-assisted protein crystallization remains a comparatively rare undertaking, the number of crystal structures of polypeptides fused to maltose-binding protein (MBP) that have been deposited in the Protein Data Bank (PDB) has grown dramatically during the past decade. Altogether, 102 fusion protein structures were detected by Basic Local Alignment Search Tool (BLAST) analysis. Collectively, these structures comprise a range of sizes, space groups, and resolutions that are typical of the PDB as a whole. While most of these MBP fusion proteins were equipped with short inter-domain linkers to increase their rigidity, fusion proteins with long linkers have also been crystallized. In some cases, surface entropy reduction mutations in MBP appear to have facilitated the formation of crystals. A comparison of the structures of fused and unfused proteins, where both are available, reveals that MBP-mediated structural distortions are very rare.

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Section: Methodsmentioning

confidence: 99%

Crystal structures of MBP fusion proteins

Waugh

2016

Protein Science

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Computer program (SEQPEP) to aid in the interpretation of high-energy collision tandem mass spectra of peptides

Johnson

Biemann

1989

Biol. Mass Spectrom.

116

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An algorithm (SEQPEP) that aids in the interpretation of high-energy (greater than 1 kV) collision-induced dissociation mass spectra of peptide ions generated by fast atom bombardment (FAB) ionization is described. The only required input is a list of product ion masses and relative abundances generated by the mass spectrometer data system, the mass of the precursor [M + H]+ ion, and the mass of any C-terminal modification, if present (e.g., amide). Possible N-terminal modifications and amino acid compositions are not required as input. In the output, sequences are ranked according to the fraction of total product ion current that can be accounted for as either sequence-specific or non-sequence-specific fragment ions. These are listed by ion type. One of the major advantages of this program over algorithms described earlier is the incorporation of ion types more recently discovered. Also, this program is much faster, requiring less than 5 min of central processing unit time for an input of as many as 100 product ions. The results obtained from 50 peptides, including some generated when sequencing a protein of previously unknown structure, are discussed.

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The CXXC motif: imperatives for the formation of native disulfide bonds in the cell.

1996

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The rapid formation of native disulfide bonds in cellular proteins is necessary for the efficient use of cellular resources. This process is catalyzed in vitro by protein disulfide isomerase (PDI), with the PDI1 gene being essential for the viability of Saccharomyces cerevisiae. PDI is a member of the thioredoxin (Trx) family of proteins, which have the active‐site motif CXXC. PDI contains two Trx domains as well as two domains unrelated to the Trx family. We find that the gene encoding Escherichia coli Trx is unable to complement PDI1 null mutants of S.cerevisiae. Yet, Trx can replace PDI if it is mutated to have a CXXC motif with a disulfide bond of high reduction potential and a thiol group of low pKa. Thus, an enzymic thiolate is both necessary and sufficient for the formation of native disulfide bonds in the cell.

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Nucleotide sequence of the thioredoxin gene from Escherichia coli

Cited by 39 publications

References 26 publications

Crystal structures of MBP fusion proteins

Crystal structures of MBP fusion proteins

Computer program (SEQPEP) to aid in the interpretation of high-energy collision tandem mass spectra of peptides

The CXXC motif: imperatives for the formation of native disulfide bonds in the cell.

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