Journal article icon

Journal article

1H, 13C and 15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli

Abstract:

Viability and pathogenicity of Gram-negative bacteria is linked to the cytochrome c maturation and the oxidative protein folding systems in the periplasm. The transmembrane reductant conductor DsbD is a unique protein which provides the necessary reducing power to both systems through thiol-disulfide exchange reactions in a complex network of protein-protein interactions. The N-terminal domain of DsbD (nDsbD) is the delivery point of the reducing power originating from cytoplasmic thioredoxin...

Expand abstract
Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

Actions


Access Document


Files:
Publisher copy:
10.1007/s12104-011-9347-9

Authors


More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
More from this funder
Funding agency for:
Ferguson, SJ
More from this funder
Funding agency for:
Redfield, C
Publisher:
Springer Netherlands Publisher's website
Journal:
Biomolecular NMR Assignments Journal website
Volume:
6
Issue:
2
Pages:
163-167
Publication date:
2011-01-01
DOI:
EISSN:
1874-270X
ISSN:
1874-2718
URN:
uuid:d2934bd7-e5f7-4efb-9f5b-b3cbc2c7d0bd
Source identifiers:
216518
Local pid:
pubs:216518

Terms of use


Metrics


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP