Chemical shift assignments of a reduced N-terminal truncation mutant of the disulfide bond isomerase TrbB from plasmid F, TrbBΔ29

التفاصيل البيبلوغرافية
العنوان: Chemical shift assignments of a reduced N-terminal truncation mutant of the disulfide bond isomerase TrbB from plasmid F, TrbBΔ29
المؤلفون: Joel F. Schildbach, Ananya Majumdar, Nathan T. Wright, Casey W. Hemmis
المصدر: Biomolecular NMR Assignments. 8:435-438
بيانات النشر: Springer Science and Business Media LLC, 2014.
سنة النشر: 2014
مصطلحات موضوعية: biology, Chemistry, Bacterial conjugation, Mutant, Protein Disulfide-Isomerases, Disulfide bond, Active site, Periplasmic space, Isomerase, Biochemistry, Article, F Factor, Plasmid, Structural Biology, biology.protein, Amino Acid Sequence, Nuclear Magnetic Resonance, Biomolecular, Peptide sequence, Sequence Deletion
الوصف: TrbB from the conjugative plasmid F is a 181-residue disulfide bond isomerase that plays a role in the correct folding and maintenance of disulfide bonds within F plasmid encoded proteins in the bacterial periplasm. As a member of the thioredoxin-like superfamily, TrbB has a predicted thioredoxin-like fold that contains a C-X-X-C active site required for performing specific redox chemistries on protein substrates. Here we report the sequence-specific assignments of the reduced form of the N-terminally truncated TrbB construct, TrbBΔ29.
تدمد: 1874-270X
1874-2718
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78b6ed809c31dded85dcaad71ed6227e
https://doi.org/10.1007/s12104-013-9533-z
حقوق: OPEN
رقم الأكسشن: edsair.doi.dedup.....78b6ed809c31dded85dcaad71ed6227e
قاعدة البيانات: OpenAIRE