Crystal structure of a PCP/Sfp complex reveals the structural basis for carrier protein posttranslational modification.
Chem Biol
; 21(4): 552-562, 2014 Apr 24.
Article
in En
| MEDLINE
| ID: mdl-24704508
ABSTRACT
Phosphopantetheine transferases represent a class of enzymes found throughout all forms of life. From a structural point of view, they are subdivided into three groups, with transferases from group II being the most widespread. They are required for the posttranslational modification of carrier proteins involved in diverse metabolic pathways. We determined the crystal structure of the group II phosphopantetheine transferase Sfp from Bacillus in complex with a substrate carrier protein in the presence of coenzyme A and magnesium, and observed two protein-protein interaction sites. Mutational analysis showed that only the hydrophobic contacts between the carrier protein's second helix and the C-terminal domain of Sfp are essential for their productive interaction. Comparison with a similar structure of a complex of human proteins suggests that the mode of interaction is highly conserved in all domains of life.
Full text:
1
Database:
MEDLINE
Main subject:
Bacterial Proteins
/
Carrier Proteins
/
Protein Processing, Post-Translational
/
Transferases (Other Substituted Phosphate Groups)
Limits:
Humans
Language:
En
Year:
2014
Type:
Article