1smb
From Proteopedia
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| - | [[Image:1smb.gif|left|200px]] | + | [[Image:1smb.gif|left|200px]] |
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| - | '''Crystal Structure of Golgi-Associated PR-1 protein''' | + | {{Structure |
| + | |PDB= 1smb |SIZE=350|CAPTION= <scene name='initialview01'>1smb</scene>, resolution 1.55Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= CAC12812 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of Golgi-Associated PR-1 protein''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1SMB is a [ | + | 1SMB is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15123429 15123429] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: alpha-beta-alpha]] | [[Category: alpha-beta-alpha]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:06:48 2008'' |
Revision as of 12:06, 20 March 2008
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| , resolution 1.55Å | |||||||
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| Gene: | CAC12812 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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