Protein Family Models

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]. [1]. 22308410. Ribosome clearance by FusB-type proteins mediates resistance to the antibiotic fusidic acid. Cox G, Thompson GS, Jenkins HT, Peske F, Savelsbergh A, Rodnina MV, Wintermeyer W, Homans SW, Edwards TA, O'Neill AJ;. Proc Natl Acad Sci U S A. 2012;109:2102-2107. [2]. 22645663. Structure and function of FusB: an elongation factor G-binding fusidic acid resistance protein active in ribosomal translocation and recycling. Guo X, Peisker K, Backbro K, Chen Y, Koripella RK, Mandava CS, Sanyal S, Selmer M;. Open Biol. 2012;2:120016. (from Pfam)

Date:

2024-10-16

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]. [1]. 11023185. Cloning, sequencing and characterisation of a Listeria monocytogenes gene encoding a fibronectin-binding protein. Gilot P, Jossin Y, Content J;. J Med Microbiol 2000;49:887-896. [2]. 22308410. Ribosome clearance by FusB-type proteins mediates resistance to the antibiotic fusidic acid. Cox G, Thompson GS, Jenkins HT, Peske F, Savelsbergh A, Rodnina MV, Wintermeyer W, Homans SW, Edwards TA, O'Neill AJ;. Proc Natl Acad Sci U S A. 2012;109:2102-2107. [3]. 22645663. Structure and function of FusB: an elongation factor G-binding fusidic acid resistance protein active in ribosomal translocation and recycling. Guo X, Peisker K, Backbro K, Chen Y, Koripella RK, Mandava CS, Sanyal S, Selmer M;. Open Biol. 2012;2:120016. [4]. 24277045. A novel staphylococcal cassette chromosomal element, SCCfusC, carrying fusC and speG in fusidic acid-resistant methicillin-resistant Staphylococcus. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

fusidic acid resistance FusB/FusC family elongation factor G-binding protein simialr to FusB/FusC that mediates resistance to the antibiotic fusidic acid and interacts with EF-G with high affinity, promoting the dissociation of stalled ribosome/EF-G/GDP complexes that form in the presence of fusidic acid, thus allowing the ribosomes to resume translation

Date:

2019-11-29