PDBsum entry 4le9

Transferase

PDB id: 4le9

Contents

Protein chain

59 a.a.

Ligands

PGE

Waters ×62

PDB id:

4le9

Name:

Transferase

Title:

Crystal structure of a chimeric c-src-sh3 domain

Structure:

Proto-oncogene tyrosine-protein kinase src. Chain: a. Fragment: unp residues 85-141. Synonym: proto-oncogenE C-src, pp60c-src, p60-src. Engineered: yes. Mutation: yes

Source:

Gallus gallus. Bantam,chickens. Organism_taxid: 9031. Gene: src. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.34Å R-factor: 0.137 R-free: 0.164

Authors:

A.Camara-Artigas,S.Martinez-Rodriguez,E.Ortiz-Salmeron,J.M.Martin- Garcia

Key ref:

A.Cámara-Artigas et al. (2014). 3D domain swapping in a chimeric c-Src SH3 domain takes place through two hinge loops. J Struct Biol, 186, 195-203. PubMed id: 24556574 DOI: 10.1016/j.jsb.2014.02.007

Date:

25-Jun-13 Release date: 07-May-14

Protein chain

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

Seq: 533 a.a.

Struc: 59 a.a.*

* PDB and UniProt seqs differ at 11 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.2014.02.007

J Struct Biol 186:195-203 (2014)

PubMed id: 24556574

3D domain swapping in a chimeric c-Src SH3 domain takes place through two hinge loops.

A.Cámara-Artigas, S.Martínez-Rodríguez, E.Ortiz-Salmerón, J.M.Martín-García.

ABSTRACT

In the Src Homology 3 domain (SH3) the RT and n-Src loops form a pocket that accounts for the specificity and affinity in binding of proline rich motifs (PRMs), while the distal and diverging turns play a key role in the folding of the protein. We have solved the structure of a chimeric mutant c-Src-SH3 domain where specific residues at the RT- and n-Src-loops have been replaced by those present in the corresponding Abl-SH3 domain. Crystals of the chimeric protein show a single molecule in the asymmetric unit, which appears in an unfolded-like structure that upon generation of the symmetry related molecules reveals the presence of a domain swapped dimer where both, RT- and n-Src loops, act as hinge loops. In contrast, the fold of the diverging type II β-turn and the distal loop are well conserved. Our results are the first evidence for the presence of a structured diverging type II β-turn in an unfolded-like intermediate of the c-Src-SH3 domain, which can be stabilized by interactions from the β-strands of the same polypeptide chain or from a neighboring one. Futhermore, this crystallographic structure opens a unique opportunity to study the effect of the amino acid sequence of the hinge loops on the 3D domain swapping process of c-Src-SH3.