5AOR

Structure of MLE RNA ADP AlF4 complex

Summary for 5AOR

• Entry DOI: 10.2210/pdb5aor/pdb
• Descriptor: DOSAGE COMPENSATION REGULATOR, 5'-R(*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP)-3', ADENOSINE-5'-DIPHOSPHATE, ... (7 entities in total)
• Functional Keywords: hydrolase-rna complex, helicase, dosage compensation, mle, deah, rox, hydrolase/rna
• Biological source: DROSOPHILA MELANOGASTER (FRUIT FLY); More
• Cellular location: Nucleus : P24785
• Total number of polymer chains: 4
• Total formula weight: 295636.47

Authors

Prabu, J.R.,Conti, E. (deposition date: 2015-09-11, release date: 2015-11-18, Last modification date: 2024-01-10)

Primary citation

Prabu, J.R.,Muller, M.,Thomae, A.W.,Schussler, S.,Bonneau, F.,Becker, P.B.,Conti, E.
Structure of the RNA Helicase Mle Reveals the Molecular Mechanisms for Uridine Specificity and RNA-ATP Coupling.
Mol.Cell, 60:487-, 2015

PubMed Abstract: The MLE helicase remodels the roX lncRNAs, enabling the lncRNA-mediated assembly of the Drosophila dosage compensation complex. We identified a stable MLE core comprising the DExH helicase module and two auxiliary domains: a dsRBD and an OB-like fold. MLEcore is an unusual DExH helicase that can unwind blunt-ended RNA duplexes and has specificity for uridine nucleotides. We determined the 2.1 Å resolution structure of MLEcore bound to a U10 RNA and ADP-AlF4. The OB-like and dsRBD folds bind the DExH module and contribute to form the entrance of the helicase channel. Four uridine nucleotides engage in base-specific interactions, rationalizing the conservation of uridine-rich sequences in critical roX substrates. roX2 binding is orchestrated by MLE's auxiliary domains, which is prerequisite for MLE localization to the male X chromosome. The structure visualizes a transition-state mimic of the reaction and suggests how eukaryotic DEAH/RHA helicases couple ATP hydrolysis to RNA translocation.

PubMed: 26545078
DOI: 10.1016/J.MOLCEL.2015.10.011

Experimental method

X-RAY DIFFRACTION (2.08 Å)