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Research works show that N-terminal and full-length DrrA shows AMPylators activity toward host's Rab1b protein (Ras related protein), which is also the substrate of Rab1b GEF domain. Rab1b protein is the GTPase Rab to regulate vesicle transportation and membrane fusion. The adenylation by bacteria AMPylators prolong GTP-bound state of Rab1b.
The adenylation domain (A) is the focus for substrate specificity since it is the initiating and substrate recognition domain. In one example, adenylation substrate-binding pocket (defined by 10 residue within) alignments led to clusters giving rise to defined specificity (i.e. the residues of the enzyme pocket can predict nonribosomal peptide ...
Poly(A)-binding protein is exported to the cytoplasm with the RNA. mRNAs that are not exported are degraded by the exosome. [39] [40] Poly(A)-binding protein also can bind to, and thus recruit, several proteins that affect translation, [39] one of these is initiation factor-4G, which in turn recruits the 40S ribosomal subunit. [41]
Uba2 subunit is 640 aa residues long with a molecular weight of 72 kDa. [8] It consists of three domains: an adenylation domain (containing adenylation active site), a catalytic Cys domain (containing the catalytic Cys173 residue participated in thioester bond formation), and a ubiquitin-like domain.
Identified proteins that are coordinated by CPSF activity include: cleavage stimulatory factor and the two poorly understood cleavage factors. The binding of the polynucleotide adenylyltransferase responsible for actually synthesizing the tail is a necessary prerequisite for cleavage, thus ensuring that cleavage and polyadenylation are tightly ...
A typical elongation module consists of an adenylation domain (A), a peptidyl carrier protein domain (PCP) and a condensation domain (C). Some other domains may be present that are responsible for modifications to the residues, such as epimerization domain (E) and N-methyltransferase domain (MT).
Within the biosynthetic pathway, there are total of five modules that specifically recognize, activate, and condense the amino acids to gramicidin S. Starting module GrsA consists of three domains: Adenylation (A) domain where it incorporates the amino acid and activates it by adenylation using ATP, Thiolation (T) domain or peptidyl carrier ...
Loading: The first amino acid is activated with ATP as a mixed acyl-phosphoric acid anhydride with AMP by the A-domain and loaded onto the serine-attached 4'-phospho-pantethine (4'PP) sidechain of the PCP-domain catalyzed by the PCP-domain (thiolation). Some A domains require interaction with MbtH-like proteins for their activity. [8] [9]