2JWN

Solution NMR structure of the protease-resistent domain of Xenopus laevis ePABP2

Summary for 2JWN

• Entry DOI: 10.2210/pdb2jwn/pdb
• NMR Information: BMRB: 15528
• Descriptor: Embryonic polyadenylate-binding protein 2-B (1 entity in total)
• Functional Keywords: epabp2, poly(a) binding, structural genomics, protein structure initiative, psi-2, center for eukaryotic structural genomics, cytoplasm rna-binding, cesg, rna binding protein
• Biological source: Xenopus laevis (African clawed frog)
• Cellular location: Cytoplasm: Q6TY21
• Total number of polymer chains: 2
• Total formula weight: 27102.51

Authors

Song, J.,Markley, J.L.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2007-10-16, release date: 2007-10-30, Last modification date: 2024-05-29)

Primary citation

Song, J.,McGivern, J.V.,Nichols, K.W.,Markley, J.L.,Sheets, M.D.
Structural basis for RNA recognition by a type II poly(A)-binding protein.
Proc.Natl.Acad.Sci.USA, 105:15317-15322, 2008

PubMed Abstract: We identified a functional domain (XlePABP2-TRP) of Xenopus laevis embryonic type II poly(A)-binding protein (XlePABP2). The NMR structure of XlePABP2-TRP revealed that the protein is a homodimer formed by the antiparallel association of beta-strands from the single RNA recognition motif (RRM) domain of each subunit. In each subunit of the homodimer, the canonical RNA recognition site is occluded by a polyproline motif. Upon poly(A) binding, XlePABP2-TRP undergoes a dimer-monomer transition that removes the polyproline motif from the RNA recognition site and allows it to be replaced by the adenosine nucleotides of poly(A). Our results provide high-resolution structural information concerning type II PABPs and an example of a single RRM domain protein that transitions from a homodimer to a monomer upon RNA binding. These findings advance our understanding of RRM domain regulation, poly(A) recognition, and are relevant to understanding how type II PABPs function in mRNA processing and human disease.

PubMed: 18824697
DOI: 10.1073/pnas.0801274105

Experimental method

SOLUTION NMR