3bf0
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:3bf0.jpg|left|200px]] | [[Image:3bf0.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_3bf0", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_3bf0| PDB=3bf0 | SCENE= }} | |
| - | + | ||
| - | | | + | |
| - | }} | + | |
'''Crystal structure of Escherichia coli Signal peptide peptidase (SppA), Native crystals''' | '''Crystal structure of Escherichia coli Signal peptide peptidase (SppA), Native crystals''' | ||
| Line 26: | Line 23: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Paetzel, M.]] | [[Category: Paetzel, M.]] | ||
| - | [[Category: | + | [[Category: Bacterial]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | [[Category: | + | [[Category: Inner membrane]] |
| - | [[Category: | + | [[Category: Membrane]] |
| - | [[Category: | + | [[Category: Protease]] |
| - | [[Category: | + | [[Category: Ser/lys protease]] |
| - | [[Category: | + | [[Category: Transmembrane]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:42:17 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:42, 4 May 2008
Crystal structure of Escherichia coli Signal peptide peptidase (SppA), Native crystals
Overview
Signal peptide peptidase (Spp) is the enzyme responsible for cleaving the remnant signal peptides left behind in the membrane following Sec-dependent protein secretion. Spp activity appears to be present in all cell types, eukaryotic, prokaryotic and archaeal. Here we report the first structure of a signal peptide peptidase, that of the Escherichia coli SppA (SppA(EC)). SppA(EC) forms a tetrameric assembly with a novel bowl-shaped architecture. The bowl has a dramatically hydrophobic interior and contains four separate active sites that utilize a Ser/Lys catalytic dyad mechanism. Our structural analysis of SppA reveals that while in many Gram-negative bacteria as well as characterized plant variants, a tandem duplication in the protein fold creates an intact active site at the interface between the repeated domains, other species, particularly Gram-positive and archaeal organisms, encode half-size, unduplicated SppA variants that could form similar oligomers to their duplicated counterparts, but using an octamer arrangement and with the catalytic residues provided by neighboring monomers. The structure reveals a similarity in the protein fold between the domains in the periplasmic Ser/Lys protease SppA and the monomers seen in the cytoplasmic Ser/His/Asp protease ClpP. We propose that SppA may, in addition to its role in signal peptide hydrolysis, have a role in the quality assurance of periplasmic and membrane-bound proteins, similar to the role that ClpP plays for cytoplasmic proteins.
About this Structure
3BF0 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of a bacterial signal Peptide peptidase., Kim AC, Oliver DC, Paetzel M, J Mol Biol. 2008 Feb 15;376(2):352-66. Epub 2007 Dec 4. PMID:18164727 Page seeded by OCA on Sun May 4 20:42:17 2008
