PDBsum entry 5d0u

Hydrolase

PDB id: 5d0u

Contents

Protein chain

705 a.a.

Ligands

ADP

DMS ×9

Metals

_MG

Waters ×4

PDB id:

5d0u

Name:

Hydrolase

Title:

Crystal structure of the RNA-helicase prp43 from chaetomium thermophilum bound to adp

Structure:

Pre-mRNA-splicing factor atp-dependent RNA helicase prp43. Chain: a. Fragment: unp residues 61-764. Engineered: yes. Other_details: the protein was expressed with 2 additional n-terminal amino acids (ma) and a c-terminal strep-tag (wshpqfek).

Source:

Chaetomium thermophilum var. Thermophilum dsm 1495. Organism_taxid: 759272. Strain: dsm 1495 / cbs 144.50 / imi 039719. Gene: ctht_0005780. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.92Å R-factor: 0.193 R-free: 0.231

Authors:

M.J.Tauchert,R.Ficner

Key ref:

M.J.Tauchert et al. (2016). Structural and functional analysis of the RNA helicase Prp43 from the thermophilic eukaryote Chaetomium thermophilum. Acta Crystallogr F Struct Biol Commun, 72, 112-120. PubMed id: 26841761 DOI: 10.1107/S2053230X15024498

Date:

03-Aug-15 Release date: 10-Feb-16

Protein chain

G0RY84  (G0RY84_CHATD) -  RNA helicase from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

Seq: 764 a.a.

Struc: 705 a.a.

Enzyme reactions

• Enzyme class: E.C.3.6.4.13 - Rna helicase.
• Reaction: ATP + H2O = ADP + phosphate + H⁺

ATP + H2O = ADP (Bound ligand (Het Group name = ADP) corresponds exactly) + phosphate + H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1107/S2053230X15024498

Acta Crystallogr F Struct Biol Commun 72:112-120 (2016)

PubMed id: 26841761

Structural and functional analysis of the RNA helicase Prp43 from the thermophilic eukaryote Chaetomium thermophilum.

M.J.Tauchert, J.B.Fourmann, H.Christian, R.Lührmann, R.Ficner.

ABSTRACT

RNA helicases are indispensable for all organisms in each domain of life and have implications in numerous cellular processes. The DEAH-box RNA helicase Prp43 is involved in pre-mRNA splicing as well as rRNA maturation. Here, the crystal structure of Chaetomium thermophilum Prp43 at 2.9 Å resolution is revealed. Furthermore, it is demonstrated that Prp43 from C. thermophilum is capable of functionally replacing its orthologue from Saccharomyces cerevisiae in spliceosomal disassembly assays.