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Journal of Bacteriology, July 2003, p. 4081-4086, Vol. 185, No. 14
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.14.4081-4086.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Determinants of the Src Homology Domain 3-Like Fold

J. Alejandro D'Aquino and Dagmar Ringe*

Department of Chemistry and Biochemistry and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02454

Received 19 February 2003/ Accepted 30 April 2003

In eukaryotes, the Src homology domain 3 (SH3) is a very important motif in signal transduction. SH3 domains recognize poly-proline-rich peptides and are involved in protein-protein interactions. Until now, the existence of SH3 domains has not been demonstrated in prokaryotes. However, the structure of the C-terminal domain of DtxR clearly shows that the fold of this domain is very similar to that of the SH3 domain. In addition, there is evidence that the C-terminal domain of DtxR binds to poly-proline-rich regions. Other bacterial proteins have domains that are structurally similar to the SH3 domain but whose functions are unknown or differ from that of the SH3 domain. The observed similarities between the structures of the C-terminal domain of DtxR and the SH3 domain constitute a perfect system to gain insight into their function and information about their evolution. Our results show that the C-terminal domain of DtxR shares a number of conserved key hydrophobic positions not recognizable from sequence comparison that might be responsible for the integrity of the SH3-like fold. Structural alignment of an ensemble of such domains from unrelated proteins shows a common structural core that seems to be conserved despite the lack of sequence similarity. This core constitutes the minimal requirements of protein architecture for the SH3-like fold.

* Corresponding author. Mailing address: Department of Chemistry and Biochemistry and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02454. Phone: (781) 736-4902. Fax: (781) 736-2405. E-mail: ringe{at}brandeis.edu.

Journal of Bacteriology, July 2003, p. 4081-4086, Vol. 185, No. 14
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.14.4081-4086.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • D'Aquino, J. A., Tetenbaum-Novatt, J., White, A., Berkovitch, F., Ringe, D. (2005). Mechanism of metal ion activation of the diphtheria toxin repressor DtxR. Proc. Natl. Acad. Sci. USA 102: 18408-18413 [Abstract] [Full Text]  
  • Manabe, Y. C., Hatem, C. L., Kesavan, A. K., Durack, J., Murphy, J. R. (2005). Both Corynebacterium diphtheriae DtxR(E175K) and Mycobacterium tuberculosis IdeR(D177K) Are Dominant Positive Repressors of IdeR-Regulated Genes in M. tuberculosis. Infect. Immun. 73: 5988-5994 [Abstract] [Full Text]  


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