1smb
From Proteopedia
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Crystal Structure of Golgi-Associated PR-1 protein
Overview
The plant pathogenesis related proteins group 1 (PR-1) and a variety of, related mammalian proteins constitute a PR-1 protein family that share, sequence and structural similarities. GAPR-1 is a unique family member as, thus far it is the only PR-1 family member that is not co-translationally, targeted to the lumen of the endoplasmic reticulum before trafficking to, either vacuoles or secretion. Here we report that GAPR-1 may form dimers, in vitro and in vivo, as determined by yeast two-hybrid screening, biochemical and biophysical assays. The 1.55A crystal structure, demonstrates that GAPR-1 is structurally homologous to the other PR-1, family members previously solved (p14a and Ves V 5). Through an, examination of inter-molecular interactions between GAPR-1 molecules in, the crystal lattice, we propose a number of the highly conserved amino, acid residues of the PR-1 family to be involved in the regulation of dimer, formation of GAPR-1 with potential implications for other PR-1 family, members. We show that mutagenesis of these conserved amino acid residues, leads to a greatly increased dimer population. A recent report suggests, that PR-1 family members may exhibit serine protease activity and further, examination of the dimer interface of GAPR-1 indicates that a catalytic, triad similar to that of serine proteases may be formed across the dimer, interface by residues from both molecules within the dimer.
About this Structure
1SMB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural analysis of the human Golgi-associated plant pathogenesis related protein GAPR-1 implicates dimerization as a regulatory mechanism., Serrano RL, Kuhn A, Hendricks A, Helms JB, Sinning I, Groves MR, J Mol Biol. 2004 May 21;339(1):173-83. PMID:15123429
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