2LHN
RNA-binding zinc finger protein
Summary for 2LHN
Entry DOI | 10.2210/pdb2lhn/pdb |
NMR Information | BMRB: 17858 |
Descriptor | Nuclear polyadenylated RNA-binding protein NAB2, ZINC ION (2 entities in total) |
Functional Keywords | rna-binding protein, nuclear protein |
Biological source | Saccharomyces cerevisiae S288c (Baker's yeast) |
Cellular location | Nucleus: P32505 |
Total number of polymer chains | 1 |
Total formula weight | 9424.02 |
Authors | Brockmann, C.,Neuhaus, D.,Stewart, M. (deposition date: 2011-08-12, release date: 2012-06-27, Last modification date: 2024-05-01) |
Primary citation | Brockmann, C.,Soucek, S.,Kuhlmann, S.I.,Mills-Lujan, K.,Kelly, S.M.,Yang, J.C.,Iglesias, N.,Stutz, F.,Corbett, A.H.,Neuhaus, D.,Stewart, M. Structural Basis for Polyadenosine-RNA Binding by Nab2 Zn Fingers and Its Function in mRNA Nuclear Export. Structure, 20:1007-1018, 2012 Cited by PubMed Abstract: Polyadenylation regulation and efficient nuclear export of mature mRNPs both require the polyadenosine-RNA-binding protein, Nab2, which contains seven CCCH Zn fingers. We describe here the solution structure of fingers 5-7, which are necessary and sufficient for high-affinity polyadenosine-RNA binding, and identify key residues involved. These Zn fingers form a single structural unit. Structural coherence is lost in the RNA-binding compromised Nab2-C437S mutant, which also suppresses the rat8-2 allele of RNA helicase Dbp5. Structure-guided Nab2 variants indicate that dbp5(rat8-2) suppression is more closely linked to hyperadenylation and suppression of mutant alleles of the nuclear RNA export adaptor, Yra1, than to affinity for polyadenosine-RNA. These results indicate that, in addition to modulating polyA tail length, Nab2 has an unanticipated function associated with generating export-competent mRNPs, and that changes within fingers 5-7 lead to suboptimal assembly of mRNP export complexes that are more easily disassembled by Dbp5 upon reaching the cytoplasm. PubMed: 22560733DOI: 10.1016/j.str.2012.03.011 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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