3bf0: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:3bf0.jpg|left|200px]]
{{Seed}}
[[Image:3bf0.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3bf0|  PDB=3bf0  |  SCENE=  }}  
{{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===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_18164727}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 18164727 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_18164727}}


==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Ser/lys protease]]
[[Category: Ser/lys protease]]
[[Category: Transmembrane]]
[[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 Sun Jul 27 12:23:26 2008''

Revision as of 09:23, 27 July 2008

File:3bf0.png

Template:STRUCTURE 3bf0

Crystal structure of Escherichia coli Signal peptide peptidase (SppA), Native crystals

Template:ABSTRACT PUBMED 18164727

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 Jul 27 12:23:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=3bf0&oldid=645809"