The structure of Resuscitation promoting factor B from M. tuberculosis reveals unexpected ubiquitin-like domains.
Biochim Biophys Acta
; 1860(2): 445-51, 2016 Feb.
Article
in En
| MEDLINE
| ID: mdl-26549874
ABSTRACT
BACKGROUND:
RpfB is a key factor in resuscitation from dormancy of Mycobacterium tuberculosis. This protein is a cell-wall glycosidase, which cleaves cell-wall peptidoglycan. RpfB is structurally complex and is composed of three types of domains, including a catalytic, a G5 and three DUF348 domains. Structural information is currently limited to a portion of the protein including only the catalytic and G5 domains. To gain insights into the structure and function of all domains we have undertaken structural investigations on a large protein fragment containing all three types of domains that constitute RpfB (RpfB3D).METHODS:
The structural features of RpfB3D have been investigated combining x-ray crystallography and biophysical studies. RESULTS ANDCONCLUSIONS:
The crystal structure of RpfB3D provides the first structural characterization of a DUF348 domain and revealed an unexpected structural relationship with ubiquitin. The crystal structure also provides specific structural features of these domains explaining their frequent association with G5 domains. GENERALSIGNIFICANCE:
Results provided novel insights into the mechanism of peptidoglycan degradation necessary to the resuscitation of M. tuberculosis. Features of the DUF348 domain add structural data to a large set of proteins embedding this domain. Based on its structural similarity to ubiquitin and frequent association to the G5 domain, we propose to name this domain as G5-linked-Ubiquitin-like domain, UBLG5.Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bacterial Proteins
/
Ubiquitin
/
Mycobacterium tuberculosis
Language:
En
Journal:
Biochim Biophys Acta
Year:
2016
Type:
Article
Affiliation country:
Italy