1OF5

Crystal structure of Mex67-Mtr2

Summary for 1OF5

• Entry DOI: 10.2210/pdb1of5/pdb
• Descriptor: MRNA EXPORT FACTOR MEX67, MRNA TRANSPORT REGULATOR MTR2, MERCURY (II) ION, ... (4 entities in total)
• Functional Keywords: transport, mrna transport, nuclear protein, leucine- rich repeat, nuclear transport
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Total number of polymer chains: 2
• Total formula weight: 45919.58

Authors

Fribourg, S.,Conti, E. (deposition date: 2003-04-08, release date: 2003-07-03, Last modification date: 2024-05-08)

Primary citation

Fribourg, S.,Conti, E.
Structural similarity in the absence of sequence homology of the messenger RNA export factors Mtr2 and p15.
EMBO Rep., 4:699-703, 2003

PubMed Abstract: The association between Mtr2 and Mex67 is essential for the nuclear export of bulk messenger RNA in yeast. In metazoans, the analogous function is carried out by the TAP-p15 heterodimer. Whereas Mex67 and TAP are highly conserved proteins, their binding partners, Mtr2 and p15, share no sequence similarity, but are nevertheless functionally homologous. Here, we report the 2.8-A resolution crystal structure of Mtr2 in complex with the NTF2-like domain of Mex67. Mtr2 is a novel member of the NTF2-like family and interacts with Mex67, forming a complex with a similar structural architecture to that of TAP-p15. Mtr2 fulfils an analogous function to that of human p15 in maintaining the structural integrity of the heterodimer. In addition, Mtr2 presents a long internal loop, which contains residues that affect the export of the large ribosomal subunit.

PubMed: 12835756
DOI: 10.1038/sj.embor.embor883

Experimental method

X-RAY DIFFRACTION (2.8 Å)