1p92
From Proteopedia
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Crystal Structure of (H79A)DtxR
Overview
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.
About this Structure
1P92 is a Single protein structure of sequence from Corynebacterium diphtheriae with BME as ligand. Full crystallographic information is available from OCA.
Reference
Determinants of the SRC homology domain 3-like fold., D'Aquino JA, Ringe D, J Bacteriol. 2003 Jul;185(14):4081-6. PMID:12837782
Page seeded by OCA on Tue Nov 20 23:36:31 2007
