Characterizing a novel CMK-EngA fusion protein from Bifidobacterium: Implications for inter-domain regulation.
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ABSTRACT: EngA is an essential and unique bacterial GTPase involved in ribosome biogenesis. The essentiality and species-specific variations among EngA homologues make the protein a potential target for future drug development. In this aspect, it is important to understand the variations of EngA among probiotic organisms and non-probiotic bacteria to understand species specificity. The search for variations among EngA homologues revealed a unique variant, exclusively found in Bifidobacterium and a few Actinobacteria species. Bifidobacterium possesses a multifunctional fusion protein, wherein EngA is fused with an N-terminal CMK (Cytidylate Monophosphate Kinase) domain. The resulting protein is therefore a large (70kDa size) with 3 consecutive P-loops and a 50 amino acid long lin
SUBMITTER: Suresh A
PROVIDER: S-EPMC9791819 | biostudies-literature | 2023 Mar
REPOSITORIES: biostudies-literature
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