PDBsum entry 4prf

RNA binding protein/RNA

PDB id: 4prf

Contents

Protein chain

95 a.a.

DNA/RNA

Metals

_SR ×2

Waters ×42

PDB id:

4prf

Name:

RNA binding protein/RNA

Title:

A second look at the hdv ribozyme structure and dynamics.

Structure:

Hepatitis delta virus ribozyme. Chain: b. Engineered: yes. U1 small nuclear ribonucleoprotein a. Chain: a. Fragment: u1a_rbd, unp residues 98-173. Synonym: u1 snrnp a, u1-a, u1a. Engineered: yes. Mutation: yes

Source:

Synthetic: yes. Other_details: RNA occurs from hapatitis delta virus pathogen, in vitro transcription with puc19. Homo sapiens. Human. Organism_taxid: 9606. Gene: snrpa. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.40Å R-factor: 0.201 R-free: 0.252

Authors:

G.J.Kapral,S.Jain,J.Noeske,J.A.Doudna,D.C.Richardson,J.S.Richardson

Key ref:

G.J.Kapral et al. (2014). New tools provide a second look at HDV ribozyme structure, dynamics and cleavage. Nucleic Acids Res, 42, 12833-12846. PubMed id: 25326328 DOI: 10.1093/nar/gku992

Date:

05-Mar-14 Release date: 29-Oct-14

Supersedes:

1vc7

Protein chain

P09012  (SNRPA_HUMAN) -  U1 small nuclear ribonucleoprotein A from Homo sapiens

Seq: 282 a.a.

Struc: 95 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DNA/RNA chain

A-U-G-G-C-C-G-G-C-A-U-G-G-U-C-C-C-A-G-C-C-U-C-C-U-C-G-C-U-G-G-C-G-C-C-G-G-C-U- 74 bases

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1093/nar/gku992

Nucleic Acids Res 42:12833-12846 (2014)

PubMed id: 25326328

New tools provide a second look at HDV ribozyme structure, dynamics and cleavage.

G.J.Kapral, S.Jain, J.Noeske, J.A.Doudna, D.C.Richardson, J.S.Richardson.

ABSTRACT

The hepatitis delta virus (HDV) ribozyme is a self-cleaving RNA enzyme essential for processing viral transcripts during rolling circle viral replication. The first crystal structure of the cleaved ribozyme was solved in 1998, followed by structures of uncleaved, mutant-inhibited and ion-complexed forms. Recently, methods have been developed that make the task of modeling RNA structure and dynamics significantly easier and more reliable. We have used ERRASER and PHENIX to rebuild and re-refine the cleaved and cis-acting C75U-inhibited structures of the HDV ribozyme. The results correct local conformations and identify alternates for RNA residues, many in functionally important regions, leading to improved R values and model validation statistics for both structures. We compare the rebuilt structures to a higher resolution, trans-acting deoxy-inhibited structure of the ribozyme, and conclude that although both inhibited structures are consistent with the currently accepted hammerhead-like mechanism of cleavage, they do not add direct structural evidence to the biochemical and modeling data. However, the rebuilt structures (PDBs: 4PR6, 4PRF) provide a more robust starting point for research on the dynamics and catalytic mechanism of the HDV ribozyme and demonstrate the power of new techniques to make significant improvements in RNA structures that impact biologically relevant conclusions.