Functional and evolutionary analyses of Helicobacter pylori HP0231 (DsbK) protein with strong oxidative and chaperone activity characterized by a highly diverged dimerization domain

Functional and evolutionary analyses of Helicobacter pylori HP0231 (DsbK) protein with strong oxidative and chaperone activity characterized by a highly diverged dimerization domain

Helicobacter pylori does not encode the classical DsbA/DsbB oxidoreductases that are crucial for oxidative folding of extracytoplasmic proteins. Instead, this microorganism encodes an untypical two proteins playing a role in disulfide bond formation – periplasmic HP0231, which structure resembles th...

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Bibliographic Details
Main Authors: Katarzyna Marta Bocian-Ostrzycka, Anna Maria Łasica, Stanisław eDunin-Horkawicz, Magdalena Joanna Grzeszczuk, Karolina eDrabik, Aneta Maria Dobosz, Renata eGodlewska, Elżbieta eNowak, Jean-Francois eCollet, Elżbieta Katarzyna Jagusztyn-Krynicka
Format: Article
Language:English
Published: Frontiers Media S.A. 2015-10-01
Series:Frontiers in Microbiology
Subjects:
Helicobacter pylori
disulfide bonds
chaperone activity
Dsb proteins
oxidoreductase activity
Online Access:http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.01065/full

Internet

http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.01065/full

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