PDBsum entry 2btt

Contractile protein

PDB id: 2btt

Contents

Protein chain

69 a.a. *

* Residue conservation analysis

PDB id:

2btt

Name:

Contractile protein

Title:

Nmr structure of myo3-sh3 domain from myosin-typei from s. Cerevisiae

Structure:

Myosin-3 isoform. Chain: a. Fragment: sh3 domain, residues 1122-1190. Synonym: myo3-sh3 domain, myo3-sh3 isoform. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562

NMR struc:

20 models

Authors:

V.Musi,B.Birdsall,A.Pastore

Key ref:

V.Musi et al. (2006). New approaches to high-throughput structure characterization of SH3 complexes: the example of Myosin-3 and Myosin-5 SH3 domains from S. cerevisiae. Protein Sci, 15, 795-807. PubMed id: 16600966 DOI: 10.1110/ps.051785506

Date:

06-Jun-05 Release date: 12-Apr-06

Protein chain

P36006  (MYO3_YEAST) -  Myosin-3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 1272 a.a.

Struc: 69 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1110/ps.051785506

Protein Sci 15:795-807 (2006)

PubMed id: 16600966

New approaches to high-throughput structure characterization of SH3 complexes: the example of Myosin-3 and Myosin-5 SH3 domains from S. cerevisiae.

V.Musi, B.Birdsall, G.Fernandez-Ballester, R.Guerrini, S.Salvatori, L.Serrano, A.Pastore.

ABSTRACT

SH3 domains are small protein modules that are involved in protein-protein interactions in several essential metabolic pathways. The availability of the complete genome and the limited number of clearly identifiable SH3 domains make the yeast Saccharomyces cerevisae an ideal proteomic-based model system to investigate the structural rules dictating the SH3-mediated protein interactions and to develop new tools to assist these studies. In the present work, we have determined the solution structure of the SH3 domain from Myo3 and modeled by homology that of the highly homologous Myo5, two myosins implicated in actin polymerization. We have then implemented an integrated approach that makes use of experimental and computational methods to characterize their binding properties. While accommodating their targets in the classical groove, the two domains have selectivity in both orientation and sequence specificity of the target peptides. From our study, we propose a consensus sequence that may provide a useful guideline to identify new natural partners and suggest a strategy of more general applicability that may be of use in other structural proteomic studies.

Selected figure(s)

Figure 3.
Figure 3 Relaxation parameters for Myo3-SH3 (left panel) and Myo5-SH3 (right panel) recorded at 600 MHz and 20°C. R1 and R2 and ^15N-NOE are plotted as a function of residue number. The values for the amide resonances of residues 19, 56, 57, and 64–66 for Myo3-SH3 and 2, 3, 18, 19, 57, 59, and 61 for Myo5-SH3 are missing because they were not assigned, whereas the other missing values correspond to residues that were excluded either because of overlap or because they were too weak to be properly appreciated.

Figure 5.
Figure 5 Effects of the peptide titrations on the Myo-SH3 NMR spectra. A representative example of Myo3-SH3 titrated with 3BP-1 is shown. (A) Superposition of the HSQC spectra recorded at 25°C and 500 MHz corresponding to 0, 0.33, 1, and 3 molar Myo3-SH3:peptide molar ratios colored in black, red, green, and blue, respectively. (B) Histogram of the weighted chemical shifted variation as observed for a 1:3 molar ratio of Myo3-SH3:3BP-1 complex. (C) Mapping of the interaction surface of 3BP-1 onto the structure of Myo3-SH3. The secondary structure elements are indicated with red and yellow (the -helix) and cyan (the -sheet) solid oval ribbons. The side chains of residues with amide resonances most dramatically shifted upon binding of the peptide are explicitly shown.

The above figures are reprinted by permission from the Protein Society: Protein Sci (2006, 15, 795-807) copyright 2006.

Figures were selected by an automated process.