PDBsum entry 4qt7

Transferase/transferase activator

PDB id: 4qt7

Contents

Protein chain

60 a.a.

Ligands

ACE-ALA-PRO-PRO-ILE-PRO-PRO-PRO-ARG

Waters ×94

PDB id:

4qt7

Name:

Transferase/transferase activator

Title:

Crystal structure of thE C-src sh3 domain in complex with a peptide from the hepatitis c virus ns5a-protein

Structure:

Proto-oncogene tyrosine-protein kinase src. Chain: a. Fragment: sh3 domain, unp residues 85-141. Synonym: proto-oncogenE C-src, pp60c-src, p60-src. Engineered: yes. Ns5a. Chain: b. Fragment: proline rich peptide, unp residues 349-359. Engineered: yes

Source:

Gallus gallus. Bantam,chickens. Organism_taxid: 9031. Gene: src. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Hepatitis c virus. Organism_taxid: 11103.

Resolution:

1.55Å R-factor: 0.161 R-free: 0.195

Authors:

A.Camara-Artigas,J.Bacarizo

Key ref:

J.Bacarizo et al. (2015). Structure of the c-Src-SH3 domain in complex with a proline-rich motif of NS5A protein from the hepatitis C virus. J Struct Biol, 189, 67-72. PubMed id: 25447263 DOI: 10.1016/j.jsb.2014.11.004

Date:

07-Jul-14 Release date: 24-Dec-14

Protein chain

P00523  (SRC_CHICK) -  Proto-oncogene tyrosine-protein kinase Src from Gallus gallus

Seq: 533 a.a.

Struc: 60 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.2.7.10.2 - non-specific protein-tyrosine kinase.
• Reaction: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H⁺

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

Added reference

DOI no: 10.1016/j.jsb.2014.11.004

J Struct Biol 189:67-72 (2015)

PubMed id: 25447263

Structure of the c-Src-SH3 domain in complex with a proline-rich motif of NS5A protein from the hepatitis C virus.

J.Bacarizo, S.Martínez-Rodríguez, A.Cámara-Artigas.

ABSTRACT

The non-structural hepatitis C virus proteins NS5A and NS5B form a complex through interaction with the SH2 and SH3 domains of the non-receptor Src tyrosine kinase, which seems essential for viral replication. We have crystallized the complex between the SH3 domain of the c-Src tyrosine kinase and the C-terminal proline rich motif of the NS5A protein (A349PPIPPPRRKR359). Crystals obtained at neutral pH belong to the space group I41, with a single molecule of the SH3/NS5A complex at the asymmetric unit. The NS5A peptide is bound in a reverse orientation (class II) and the comparison of this structure with those of the high affinity synthetic peptides APP12 and VSL12 shows some important differences at the salt bridge that drives the peptide orientation. Further conformational changes in residues placed apart from the binding site also seem to play an important role in the binding orientation of this peptide. Our results show the interaction of the SH3 domain of the c-Src tyrosine kinase with a proline rich motif in the NS5A protein and point to their potential interaction in vivo.