2JPS

NAB2 N-terminal domain

Summary for 2JPS

• Entry DOI: 10.2210/pdb2jps/pdb
• Descriptor: Nuclear polyadenylated RNA-binding protein NAB2 (1 entity in total)
• Functional Keywords: protein, protein binding
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus: P32505
• Total number of polymer chains: 1
• Total formula weight: 11461.87

Authors

Grant, R.,Marshall, N.J.,Yang, J.,Fasken, M.,Kelly, S.,Harreman, M.T.,Neuhaus, D.,Corbett, A.H.,Stewart, M. (deposition date: 2007-05-23, release date: 2008-03-18, Last modification date: 2023-12-20)

Primary citation

Grant, R.P.,Marshall, N.J.,Yang, J.C.,Fasken, M.B.,Kelly, S.M.,Harreman, M.T.,Neuhaus, D.,Corbett, A.H.,Stewart, M.
Structure of the N-terminal Mlp1-binding domain of the Saccharomyces cerevisiae mRNA-binding protein, Nab2
J.Mol.Biol., 376:1048-1059, 2008

PubMed Abstract: Nuclear abundant poly(A) RNA-binding protein 2 (Nab2) is an essential yeast heterogeneous nuclear ribonucleoprotein that modulates both mRNA nuclear export and poly(A) tail length. The N-terminal domain of Nab2 (residues 1-97) mediates interactions with both the C-terminal globular domain of the nuclear pore-associated protein, myosin-like protein 1 (Mlp1), and the mRNA export factor, Gfd1. The solution and crystal structures of the Nab2 N-terminal domain show a primarily helical fold that is analogous to the PWI fold found in several other RNA-binding proteins. In contrast to other PWI-containing proteins, we find no evidence that the Nab2 N-terminal domain binds to nucleic acids. Instead, this domain appears to mediate protein:protein interactions that facilitate the nuclear export of mRNA. The Nab2 N-terminal domain has a distinctive hydrophobic patch centered on Phe73, consistent with this region of the surface being a protein:protein interaction site. Engineered mutations within this hydrophobic patch attenuate the interaction with the Mlp1 C-terminal domain but do not alter the interaction with Gfd1, indicating that this patch forms a crucial component of the interface between Nab2 and Mlp1.

PubMed: 18190927
DOI: 10.1016/j.jmb.2007.11.087

Experimental method

SOLUTION NMR