1smb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1smb.gif|left|200px]]
[[Image:1smb.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1smb |SIZE=350|CAPTION= <scene name='initialview01'>1smb</scene>, resolution 1.55&Aring;
+
The line below this paragraph, containing "STRUCTURE_1smb", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE= CAC12812 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1smb| PDB=1smb | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1smb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1smb OCA], [http://www.ebi.ac.uk/pdbsum/1smb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1smb RCSB]</span>
+
-
}}
+
'''Crystal Structure of Golgi-Associated PR-1 protein'''
'''Crystal Structure of Golgi-Associated PR-1 protein'''
Line 31: Line 28:
[[Category: Serrano, R L.]]
[[Category: Serrano, R L.]]
[[Category: Sinning, I.]]
[[Category: Sinning, I.]]
-
[[Category: alpha-beta-alpha]]
+
[[Category: Alpha-beta-alpha]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:52:48 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:44:05 2008''
+

Revision as of 05:52, 3 May 2008

Template:STRUCTURE 1smb

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 Page seeded by OCA on Sat May 3 08:52:48 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools