1H, 13C and 15N resonance assignments of the rhodanese domain of YgaP from Escherichia coli.
Biomol NMR Assign
; 5(1): 101-3, 2011 Apr.
Article
in En
| MEDLINE
| ID: mdl-20960078
ABSTRACT
Rhodanese domain is a ubiquitous structural module commonly found in bacterial, archaeal and eukaryotic cells. Growing evidence indicates that rhodanese domains act as the carrier of reactive sulfur atoms by forming persulfide intermediates in distinct metabolic pathways. YgaP, a membrane protein consisting of a rhodanese domain and a C-terminal transmembrane segment, is the only membrane-associated rhodanese in Escherichia coli. Herein, we report the resonance assignments of (1)H, (13)C and (15)N atoms of rhodanese domain of YgaP. Totally, chemical shifts of more than 95% of the atoms were assigned.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Thiosulfate Sulfurtransferase
/
Nuclear Magnetic Resonance, Biomolecular
/
Escherichia coli Proteins
/
Escherichia coli
Language:
En
Journal:
Biomol NMR Assign
Journal subject:
BIOLOGIA MOLECULAR
/
MEDICINA NUCLEAR
Year:
2011
Document type:
Article
Affiliation country: