1q40
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(New page: 200px<br /><applet load="1q40" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q40, resolution 1.95Å" /> '''Crystal structure of...)
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Revision as of 22:14, 20 November 2007
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Crystal structure of the C. albicans Mtr2-Mex67 M domain complex
Overview
The formation of the Mtr2-Mex67 heterodimer is essential for yeast mRNA, export as it constitutes a key nuclear component for shuttling mRNA, between the nuclear and cytoplasm compartments through the nuclear pore, complex. We report the crystal structures of apo-Mtr2 from the human, pathogen Candida albicans and of its complex with the Mex67 NTF2-like, domain. Compared with other members of the NTF2 fold family, Mtr2 displays, novel structural features involved in the nuclear export of the large, ribosomal subunit and consistent with a dual functional role of Mtr2, during yeast nuclear export events. The structure of the Mtr2-Mex67, NTF2-like domain complex, which overall is similar to those of the human, and Saccharomyces cerevisiae homologs, unveils three putative Phe-Gly, repeat binding sites, of which one contributes to the heterodimer, interface. These structures exemplify an unrecognized adaptability of the, NTF2 building block in evolution, identify novel structural determinants, associated with key biological functions at the molecular surface of the, yeast Mtr2-Mex67 complex, and suggest that the yeast and human mRNA export, machineries may differ.
About this Structure
1Q40 is a Protein complex structure of sequences from Candida albicans with GOL as ligand. Full crystallographic information is available from OCA.
Reference
The Mtr2-Mex67 NTF2-like domain complex. Structural insights into a dual role of Mtr2 for yeast nuclear export., Senay C, Ferrari P, Rocher C, Rieger KJ, Winter J, Platel D, Bourne Y, J Biol Chem. 2003 Nov 28;278(48):48395-403. Epub 2003 Sep 22. PMID:14504280
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