2V75

N-terminal domain of Nab2

Summary for 2V75

• Entry DOI: 10.2210/pdb2v75/pdb
• Descriptor: NUCLEAR POLYADENYLATED RNA-BINDING PROTEIN NAB2 (2 entities in total)
• Functional Keywords: metal-binding, nucleus, rna-binding, zinc-finger, nuclear protein
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Cellular location: Nucleus: P32505
• Total number of polymer chains: 1
• Total formula weight: 11390.80

Authors

Grant, R.P.,Marshall, N.J.,Stewart, M. (deposition date: 2007-07-26, release date: 2008-01-29, Last modification date: 2024-05-01)

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-, 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

X-RAY DIFFRACTION (1.8 Å)