4WWU
Structure of Mex67:Mtr2
Summary for 4WWU
| Entry DOI | 10.2210/pdb4wwu/pdb |
| Descriptor | mRNA export factor MEX67, mRNA transport regulator MTR2, ZINC ION (3 entities in total) |
| Functional Keywords | mrna nuclear export factor, transport protein |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Cellular location | Nucleus: Q99257 P34232 |
| Total number of polymer chains | 12 |
| Total formula weight | 526423.34 |
| Authors | Aibara, S.,Valkov, E.,Stewart, M. (deposition date: 2014-11-12, release date: 2015-02-04, Last modification date: 2024-05-08) |
| Primary citation | Aibara, S.,Valkov, E.,Lamers, M.,Stewart, M. Domain organization within the nuclear export factor Mex67:Mtr2 generates an extended mRNA binding surface. Nucleic Acids Res., 43:1927-1936, 2015 Cited by PubMed Abstract: The Mex67:Mtr2 complex is the principal yeast nuclear export factor for bulk mRNA and also contributes to ribosomal subunit export. Mex67 is a modular protein constructed from four domains (RRM, LRR, NTF2-like and UBA) that have been thought to be joined by flexible linkers like beads on a string, with the RRM and LRR domains binding RNAs and the NTF2-like and UBA domains binding FG-nucleoporins to facilitate movement through nuclear pores. Here, we show that the NTF2-like domain from Saccharomyces cerevisiae Mex67:Mtr2 also contributes to RNA binding. Moreover, the 3.3 Å resolution crystal structure of the Mex67(ΔUBA):Mtr2 complex, supplemented with small angle X-ray scattering data, indicated that the LRR domain has a defined spatial relationship to the Mex67(NTF2L):Mtr2 region. Conversely, the RRM domain and especially the UBA domain are more mobile. The conformation assumed by the LRR and NTF2-like domains results in clusters of positively-charged residues on each becoming arranged to form a continuous interface for binding RNA on the opposite side of the complex to the region that interacts with FG-nucleoporins to facilitate passage through nuclear pores. PubMed: 25618852DOI: 10.1093/nar/gkv030 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.301 Å) |
Structure validation
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