PDBsum entry 2wnr

Hydrolase

PDB id: 2wnr

Contents

Protein chains

261 a.a. *

222 a.a. *

210 a.a. *

Ligands

PO4 ×3

Waters ×125

* Residue conservation analysis

PDB id:

2wnr

Name:

Hydrolase

Title:

The structure of methanothermobacter thermautotrophicus exosome core assembly

Structure:

Probable exosome complex exonuclease 2. Chain: a, c, e. Engineered: yes. Probable exosome complex exonuclease 1. Chain: b, d, f. Engineered: yes

Source:

Methanothermobacter thermautotrophicus. Organism_taxid: 145262. Strain: delta h. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.65Å R-factor: 0.212 R-free: 0.251

Authors:

C.L.Ng,D.G.Waterman,A.A.Antson,M.Ortiz-Lombardia

Key ref:

C.L.Ng et al. (2010). Structure of the Methanothermobacter thermautotrophicus exosome RNase PH ring. Acta Crystallogr D Biol Crystallogr, 66, 522-528. PubMed id: 20445227

Date:

19-Jul-09 Release date: 28-Apr-10

Protein chains

O26778  (RRP42_METTH) -  Exosome complex component Rrp42 from Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)

Seq: 271 a.a.

Struc: 261 a.a.

Protein chain

O26779  (RRP41_METTH) -  Exosome complex component Rrp41 from Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)

Seq: 240 a.a.

Struc: 222 a.a.

Protein chains

O26779  (RRP41_METTH) -  Exosome complex component Rrp41 from Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)

Seq: 240 a.a.

Struc: 210 a.a.

Enzyme reactions

• Enzyme class: Chains B, D, F: E.C.3.1.13.- - ?????

Acta Crystallogr D Biol Crystallogr 66:522-528 (2010)

PubMed id: 20445227

Structure of the Methanothermobacter thermautotrophicus exosome RNase PH ring.

C.L.Ng, D.G.Waterman, A.A.Antson, M.Ortiz-Lombardía.

ABSTRACT

The core of the exosome, a versatile multisubunit RNA-processing enzyme found in archaea and eukaryotes, includes a ring of six RNase PH subunits. This basic architecture is homologous to those of the bacterial and archaeal RNase PHs and the bacterial polynucleotide phosphorylase (PNPase). While all six RNase PH monomers are catalytically active in the homohexameric RNase PH, only half of them are functional in the bacterial PNPase and in the archaeal exosome core and none are functional in the yeast and human exosome cores. Here, the crystal structure of the RNase PH ring from the exosome of the anaerobic methanogenic archaeon Methanothermobacter thermautotrophicus is described at 2.65 A resolution. Free phosphate anions were found for the first time in the active sites of the RNase PH subunits of an exosome structure and provide structural snapshots of a critical intermediate in the phosphorolytic degradation of RNA by the exosome. Furthermore, the present structure highlights the plasticity of the surfaces delineating the polar regions of the RNase PH ring of the exosome, a feature that can facilitate both interaction with the many cofactors involved in exosome function and the processive activity of this enzyme.