1H, 13C and 15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli
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-disulfid...
| Main Authors: | , , , |
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| Format: | Journal article |
| Sprog: | English |
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Springer Netherlands
2011
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| _version_ | 1826298240620822528 |
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| author | Mavridou, D Stelzl, L Ferguson, S Redfield, C |
| author_facet | Mavridou, D Stelzl, L Ferguson, S Redfield, C |
| author_sort | Mavridou, D |
| collection | OXFORD |
| description | 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 to a variety of periplasmic partners. Here we report 1H, 13C and 15N assignments for resonances of nDsbD in its oxidized and reduced states. These assignments provide the starting point for detailed investigations of the interactions of nDsbD with its protein partners. © 2011 The Author(s). |
| first_indexed | 2024-03-07T04:43:51Z |
| format | Journal article |
| id | oxford-uuid:d2934bd7-e5f7-4efb-9f5b-b3cbc2c7d0bd |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T04:43:51Z |
| publishDate | 2011 |
| publisher | Springer Netherlands |
| record_format | dspace |
| spelling | oxford-uuid:d2934bd7-e5f7-4efb-9f5b-b3cbc2c7d0bd2022-03-27T08:04:54Z 1H, 13C and 15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coliJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:d2934bd7-e5f7-4efb-9f5b-b3cbc2c7d0bdEnglishSymplectic Elements at OxfordSpringer Netherlands2011Mavridou, DStelzl, LFerguson, SRedfield, CViability 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 to a variety of periplasmic partners. Here we report 1H, 13C and 15N assignments for resonances of nDsbD in its oxidized and reduced states. These assignments provide the starting point for detailed investigations of the interactions of nDsbD with its protein partners. © 2011 The Author(s). |
| spellingShingle | Mavridou, D Stelzl, L Ferguson, S Redfield, C 1H, 13C and 15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli |
| title |
1H,
13C and
15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli |
| title_full |
1H,
13C and
15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli |
| title_fullStr |
1H,
13C and
15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli |
| title_full_unstemmed |
1H,
13C and
15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli |
| title_short |
1H,
13C and
15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli |
| title_sort | 1h 13c and 15n resonance assignments for the oxidized and reduced states of the n terminal domain of dsbd from escherichia coli |
| work_keys_str_mv | AT mavridoud 1h13cand15nresonanceassignmentsfortheoxidizedandreducedstatesofthenterminaldomainofdsbdfromescherichiacoli AT stelzll 1h13cand15nresonanceassignmentsfortheoxidizedandreducedstatesofthenterminaldomainofdsbdfromescherichiacoli AT fergusons 1h13cand15nresonanceassignmentsfortheoxidizedandreducedstatesofthenterminaldomainofdsbdfromescherichiacoli AT redfieldc 1h13cand15nresonanceassignmentsfortheoxidizedandreducedstatesofthenterminaldomainofdsbdfromescherichiacoli |