PDBsum entry 6dcl

RNA binding protein/RNA

PDB id: 6dcl

Contents

Protein chains

182 a.a.

171 a.a.

DNA/RNA

Ligands

EDO

Waters ×72

PDB id:

6dcl

Name:

RNA binding protein/RNA

Title:

Crystal structure of up1 bound to pri-mirna-18a terminal loop

Structure:

Heterogeneous nuclear ribonucleoprotein a1. Chain: a, b. Synonym: hnrnp a1,helix-destabilizing protein,single-strand RNA- binding protein,hnrnp core protein a1. Engineered: yes. RNA (5'-r( Ap Gp Up Ap Gp Ap Up Up Ap Gp C)-3'). Chain: c, d. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: hnrnpa1, hnrpa1. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 9606

Resolution:

2.50Å R-factor: 0.203 R-free: 0.228

Authors:

H.Kooshapur,M.Sattler

Key ref:

H.Kooshapur et al. (2018). Structural basis for terminal loop recognition and stimulation of pri-miRNA-18a processing by hnRNP A1. Nat Commun, 9, 2479. PubMed id: 29946118

Date:

07-May-18 Release date: 27-Jun-18

Protein chain

P09651  (ROA1_HUMAN) -  Heterogeneous nuclear ribonucleoprotein A1 from Homo sapiens

Seq: 372 a.a.

Struc: 182 a.a.

Protein chain

P09651  (ROA1_HUMAN) -  Heterogeneous nuclear ribonucleoprotein A1 from Homo sapiens

Seq: 372 a.a.

Struc: 171 a.a.

DNA/RNA chains

A-G-U-A-G-A-U-U-A-G-C 11 bases

A-G-U-A-G-A-U-U-A-G-C 11 bases

Enzyme reactions

• Enzyme class: Chains A, B: E.C.?

Nat Commun 9:2479 (2018)

PubMed id: 29946118

Structural basis for terminal loop recognition and stimulation of pri-miRNA-18a processing by hnRNP A1.

H.Kooshapur, N.R.Choudhury, B.Simon, M.Mühlbauer, A.Jussupow, N.Fernandez, A.N.Jones, A.Dallmann, F.Gabel, C.Camilloni, G.Michlewski, J.F.Caceres, M.Sattler.

ABSTRACT

Post-transcriptional mechanisms play a predominant role in the control of microRNA (miRNA) production. Recognition of the terminal loop of precursor miRNAs by RNA-binding proteins (RBPs) influences their processing; however, the mechanistic basis for how levels of individual or subsets of miRNAs are regulated is mostly unexplored. We previously showed that hnRNP A1, an RBP implicated in many aspects of RNA processing, acts as an auxiliary factor that promotes the Microprocessor-mediated processing of pri-mir-18a. Here, by using an integrative structural biology approach, we show that hnRNP A1 forms a 1:1 complex with pri-mir-18a where both RNA recognition motifs (RRMs) bind to cognate RNA sequence motifs in the terminal loop of pri-mir-18a. Terminal loop binding induces an allosteric destabilization of base-pairing in the pri-mir-18a stem that promotes its downstream processing. Our results highlight terminal loop RNA recognition by RBPs as a potential general principle of miRNA biogenesis and regulation.