PDBsum entry 2i0n

Structural protein

PDB id: 2i0n

Contents

Protein chain

80 a.a. *

* Residue conservation analysis

PDB id:

2i0n

Name:

Structural protein

Title:

Structure of dictyostelium discoideum myosin vii sh3 domain with adjacent proline rich region

Structure:

Class vii unconventional myosin. Chain: a. Fragment: sh3 domain. Engineered: yes

Source:

Dictyostelium discoideum. Organism_taxid: 44689. Gene: myoi. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

NMR struc:

20 models

Authors:

Q.Wang,M.A.Deloia,Y.Kang,C.Litchke,M.A.Titus,K.J.Walters

Key ref:

Q.Wang et al. (2007). The SH3 domain of a M7 interacts with its C-terminal proline-rich region. Protein Sci, 16, 189-196. PubMed id: 17189480 DOI: 10.1110/ps.062496807

Date:

10-Aug-06 Release date: 09-Jan-07

Protein chain

Q9U1M8  (MYOI_DICDI) -  Myosin-I heavy chain from Dictyostelium discoideum

Seq: 2357 a.a.

Struc: 80 a.a.*

* PDB and UniProt seqs differ at 8 residue positions (black crosses)

DOI no: 10.1110/ps.062496807

Protein Sci 16:189-196 (2007)

PubMed id: 17189480

The SH3 domain of a M7 interacts with its C-terminal proline-rich region.

Q.Wang, M.A.Deloia, Y.Kang, C.Litchke, N.Zhang, M.A.Titus, K.J.Walters.

ABSTRACT

Myosins play essential roles in migration, cytokinesis, endocytosis, and adhesion. They are composed of a large N-terminal motor domain with ATPase and actin binding sites and C-terminal neck and tail regions, whose functional roles and structural context in the protein are less well characterized. The tail regions of myosins I, IV, VII, XII, and XV each contain a putative SH3 domain that may be involved in protein-protein interactions. SH3 domains are reported to bind proline-rich motifs, especially "PxxP" sequences, and such interactions serve regulatory functions. The activity of Src, PI3, and Itk kinases, for example, is regulated by intramolecular interactions between their SH3 domain and internal proline-rich sequences. Here, we use NMR spectroscopy to reveal the structure of a protein construct from Dictyostelium myosin VII (DdM7) spanning A1620-T1706, which contains its SH3 domain and adjacent proline-rich region. The SH3 domain forms the signature beta-barrel architecture found in other SH3 domains, with conserved tryptophan and tyrosine residues forming a hydrophobic pocket known to bind "PxxP" motifs. In addition, acidic residues in the RT or n-Src loops are available to interact with the basic anchoring residues that are typically found in ligands or proteins that bind SH3 domains. The DdM7 SH3 differs in the hydrophobicity of the second pocket formed by the 3(10) helix and following beta-strand, which contains polar rather than hydrophobic side chains. Most unusual, however, is that this domain binds its adjacent proline-rich region at a surface remote from the region previously identified to bind "PxxP" motifs. The interaction may affect the orientation of the tail without sacrificing the availability of the canonical "PxxP"-binding surface.

Selected figure(s)

Figure 1.
Figure 1. The DdM7 SH3 domain interacts with an adjacent proline-rich region. (A) Architecture of DdM7 with the SH3 domain

The above figure is reprinted by permission from the Protein Society: Protein Sci (2007, 16, 189-196) copyright 2007.

Figure was selected by an automated process.