1SMB

Crystal Structure of Golgi-Associated PR-1 protein

Summary for 1SMB

• Entry DOI: 10.2210/pdb1smb/pdb
• Descriptor: 17kD fetal brain protein (2 entities in total)
• Functional Keywords: alpha-beta-alpha, unknown function
• Biological source: Homo sapiens (human)
• Cellular location: Golgi apparatus membrane; Lipid-anchor: Q9H4G4
• Total number of polymer chains: 1
• Total formula weight: 17340.31

Authors

Serrano, R.L.,Kuhn, A.,Hendricks, A.,Helms, J.B.,Sinning, I.,Groves, M.R. (deposition date: 2004-03-08, release date: 2004-09-14, Last modification date: 2025-03-26)

Primary citation

Serrano, R.L.,Kuhn, A.,Hendricks, A.,Helms, J.B.,Sinning, I.,Groves, M.R.
Structural analysis of the human Golgi-associated plant pathogenesis related protein GAPR-1 implicates dimerization as a regulatory mechanism
J.Mol.Biol., 339:173-183, 2004

PubMed Abstract: 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.

PubMed: 15123429
DOI: 10.1016/j.jmb.2004.03.015

Experimental method

X-RAY DIFFRACTION (1.55 Å)