Ontology highlight
ABSTRACT:
SUBMITTER: Hernandez JA
PROVIDER: S-EPMC3057858 | biostudies-literature | 2011 Feb
REPOSITORIES: biostudies-literature
Hernandez Jose A JA Phillips Aaron H AH Erbil W Kaya WK Zhao Dehua D Demuez Marie M Zeymer Cathleen C Pelton Jeffery G JG Wemmer David E DE Rubio Luis M LM
The Journal of biological chemistry 20101214 8
NafY participates in the final steps of nitrogenase maturation, having a dual role as iron-molybdenum cofactor (FeMo-co) carrier and as chaperone to the FeMo-co-deficient apo-NifDK (apo-dinitrogenase). NafY contains an N-terminal domain of unknown function (n-NafY) and a C-terminal domain (core-NafY) necessary for FeMo-co binding. We show here that n-NafY and core-NafY have very weak interactions in intact NafY. The NMR structure of n-NafY reveals that it belongs to the sterile α-motif (SAM) fam ...[more]