The NMR solution structure and function of RPA3313: a putative ribosomal transport protein from Rhodopseudomonas palustris.

ABSTRACT: Protein function elucidation often relies heavily on amino acid sequence analysis and other bioinformatics approaches. The reliance is extended to structure homology modeling for ligand docking and protein-protein interaction mapping. However, sequence analysis of RPA3313 exposes a large, unannotated class of hypothetical proteins mostly from the Rhizobiales order. In the absence of sequence and structure information, further functional elucidation of this class of proteins has been significantly hindered. A high quality NMR structure of RPA3313 reveals that the protein forms a novel split ββαβ fold with a conserved ligand binding pocket between the first β-strand and the N-terminus of the α-helix. Conserved residue analysis and protein-protein interaction prediction analyses reveal multip

SUBMITTER: Catazaro J 

PROVIDER: S-EPMC5167650 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature