FusB encodes a 2-domain zinc-binding protein that binds the ribosomal translocase EF-G, causing it to dissociate from the ribosome. This action increases the ribosomal turnover rate and confers resistance to fusidic acid. This protein is considered a FusB-type protein.
This family contains a central domain Pfam:PF00013, hence the amino and carboxyl terminal domains are stored separately. This is a minimal carboxyl-terminal domain. Some are much longer.
The S4 domain is a small domain consisting of 60-65 amino acid residues that was detected in the bacterial ribosomal protein S4, eukaryotic ribosomal S9, two families of pseudouridine synthases, a novel family of predicted RNA methylases, a yeast pro ...
The S4 domain is a small domain consisting of 60-65 amino acid residues that was detected in the bacterial ribosomal protein S4, eukaryotic ribosomal S9, two families of pseudouridine synthases, a novel family of predicted RNA methylases, a yeast protein containing a pseudouridine synthetase and a deaminase domain, bacterial tyrosyl-tRNA synthetases, and a number of uncharacterized, small proteins that may be involved in translation regulation [1]. The S4 domain probably mediates binding to RNA.
Ribosomal protein L25 is an RNA binding protein, that binds 5S rRNA. This family includes Ctc from B. subtilis Swiss:P14194, which is induced by stress.
FBP_C is a family from the C terminal end of fibronectin-binding proteins. It forms an extended four-cysteine zinc-finger with a unique structural fold. Fibronectin-binding proteins bind to elongation factor G - EF-G, which is mediated by the zinc-fi ...
FBP_C is a family from the C terminal end of fibronectin-binding proteins. It forms an extended four-cysteine zinc-finger with a unique structural fold. Fibronectin-binding proteins bind to elongation factor G - EF-G, which is mediated by the zinc-finger binding to the C-terminus of EF-G [1]. FBPs release ribosomes by competing with them for EF-G [2].
This domain can be found in the N terminus of the FusB, FusC, and FusD proteins from Staphylococcus aureus. They are elongation factor G (EF-G) binding proteins that are linked to the fusidic acid (FA) resistance in S. aureus [4,5]. The FusB protei ...
This domain can be found in the N terminus of the FusB, FusC, and FusD proteins from Staphylococcus aureus. They are elongation factor G (EF-G) binding proteins that are linked to the fusidic acid (FA) resistance in S. aureus [4,5]. The FusB proteins are two-domain metalloproteins, and this N-terminal domain forms a four-helical bundle whose helices help to stabilise the conformation of the treble-clef zinc-finger in the C-terminal domain [2]. FA is an antibiotic that binds to EF-G, preventing its release from the ribosome, thus stalling bacterial protein synthesis. The FusB proteins provide FA resistance by preventing formation or facilitating dissociation of the FA-locked EF-G-ribosome complex during elongation and ribosome recycling [3].
