4PLX

Crystal structure of the triple-helical stability element at the 3' end of MALAT1

Summary for 4PLX

• Entry DOI: 10.2210/pdb4plx/pdb
• Descriptor: Core ENE hairpin and A-rich tract from MALAT1 (2 entities in total)
• Functional Keywords: triple helix, rna stability element, malat1, long noncoding rna, rna
• Biological source: Homo sapiens
• Total number of polymer chains: 3
• Total formula weight: 73719.89

Authors

Brown, J.A.,Bulkley, D.,Wang, J.,Valenstein, M.L.,Yario, T.A.,Steitz, T.A.,Steitz, J.A. (deposition date: 2014-05-19, release date: 2014-06-25, Last modification date: 2023-12-27)

Primary citation

Brown, J.A.,Bulkley, D.,Wang, J.,Valenstein, M.L.,Yario, T.A.,Steitz, T.A.,Steitz, J.A.
Structural insights into the stabilization of MALAT1 noncoding RNA by a bipartite triple helix.
Nat.Struct.Mol.Biol., 21:633-640, 2014

PubMed Abstract: Metastasis-associated lung adenocarcinoma transcript 1 (MALAT1) is a highly abundant nuclear long noncoding RNA that promotes malignancy. A 3'-stem-loop structure is predicted to confer stability by engaging a downstream A-rich tract in a triple helix, similar to the expression and nuclear retention element (ENE) from the KSHV polyadenylated nuclear RNA. The 3.1-Å-resolution crystal structure of the human MALAT1 ENE and A-rich tract reveals a bipartite triple helix containing stacks of five and four U•A-U triples separated by a C+•G-C triplet and C-G doublet, extended by two A-minor interactions. In vivo decay assays indicate that this blunt-ended triple helix, with the 3' nucleotide in a U•A-U triple, inhibits rapid nuclear RNA decay. Interruption of the triple helix by the C-G doublet induces a 'helical reset' that explains why triple-helical stacks longer than six do not occur in nature.

PubMed: 24952594
DOI: 10.1038/nsmb.2844

Experimental method

X-RAY DIFFRACTION (3.1 Å)