PDBsum entry 4o6h

Hydrolase

PDB id: 4o6h

Contents

Protein chains

(+ 2 more) 203 a.a.

Ligands

IMD ×4

Metals

__K ×4

_ZN ×8

_MG ×4

PDB id:

4o6h

Name:

Hydrolase

Title:

2.8a crystal structure of lymphocytic choriomeningitis virus nucleoprotein c-terminal domain

Structure:

Nucleoprotein. Chain: a, b, c, d, e, f, g, h. Fragment: c-terminal domain. Synonym: nucleocapsid protein, protein n. Engineered: yes

Source:

Lymphocytic choriomeningitis virus. Lcmv. Organism_taxid: 11624. Strain: armstrong. Gene: n. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.80Å R-factor: 0.229 R-free: 0.261

Authors:

B.R.West,K.M.Hastie,E.O.Saphire

Key ref:

B.R.West et al. (2014). Structure of the LCMV nucleoprotein provides a template for understanding arenavirus replication and immunosuppression. Acta Crystallogr D Biol Crystallogr, 70, 1764-1769. PubMed id: 24914986 DOI: 10.1107/S1399004714007883

Date:

20-Dec-13 Release date: 11-Jun-14

Protein chains

P09992  (NCAP_LYCVA) -  Nucleoprotein from Lymphocytic choriomeningitis virus (strain Armstrong)

Seq: 558 a.a.

Struc: 203 a.a.

Enzyme reactions

• Enzyme class: E.C.3.1.13.- - ?????

DOI no: 10.1107/S1399004714007883

Acta Crystallogr D Biol Crystallogr 70:1764-1769 (2014)

PubMed id: 24914986

Structure of the LCMV nucleoprotein provides a template for understanding arenavirus replication and immunosuppression.

B.R.West, K.M.Hastie, E.O.Saphire.

ABSTRACT

The X-ray crystal structure of the Lymphocytic choriomeningitis virus nucleoprotein C-terminal immunosuppressive domain (LCMV NPΔ340) was determined to 2.0 Å resolution. The structure indicates that LCMV NPΔ340, like the other structurally characterized arenaviral nucleoproteins, adopts the fold of an exonuclease. This structure provides a crucial three-dimensional template for functional exploration of the replication and immunosuppression of this prototypic arenavirus.