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(New page: 200px<br /> <applet load="1smb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1smb, resolution 1.55Å" /> '''Crystal Structure o...) |
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| - | [[Image:1smb.gif|left|200px]]<br /> | + | [[Image:1smb.gif|left|200px]]<br /><applet load="1smb" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1smb" size=" | + | |
caption="1smb, resolution 1.55Å" /> | caption="1smb, resolution 1.55Å" /> | ||
'''Crystal Structure of Golgi-Associated PR-1 protein'''<br /> | '''Crystal Structure of Golgi-Associated PR-1 protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The plant pathogenesis related proteins group 1 (PR-1) and a variety of | + | 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== | ==About this Structure== | ||
| - | 1SMB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1SMB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SMB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Groves, M | + | [[Category: Groves, M R.]] |
| - | [[Category: Helms, J | + | [[Category: Helms, J B.]] |
[[Category: Hendricks, A.]] | [[Category: Hendricks, A.]] | ||
[[Category: Kuhn, A.]] | [[Category: Kuhn, A.]] | ||
| - | [[Category: Serrano, R | + | [[Category: Serrano, R L.]] |
[[Category: Sinning, I.]] | [[Category: Sinning, I.]] | ||
[[Category: alpha-beta-alpha]] | [[Category: alpha-beta-alpha]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:02:57 2008'' |
Revision as of 13:02, 21 February 2008
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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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