Source:http://linkedlifedata.com/resource/pubmed/id/18164727
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
2008-1-29
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| pubmed:databankReference | |
| pubmed:abstractText |
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.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/signal peptide peptidase
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
1089-8638
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:day |
15
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| pubmed:volume |
376
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
352-66
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| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:18164727-Amino Acid Sequence,
pubmed-meshheading:18164727-Aspartic Acid Endopeptidases,
pubmed-meshheading:18164727-Bacterial Proteins,
pubmed-meshheading:18164727-Binding Sites,
pubmed-meshheading:18164727-Catalysis,
pubmed-meshheading:18164727-Crystallography, X-Ray,
pubmed-meshheading:18164727-Escherichia coli,
pubmed-meshheading:18164727-Escherichia coli Proteins,
pubmed-meshheading:18164727-Hydrogen Bonding,
pubmed-meshheading:18164727-Models, Chemical,
pubmed-meshheading:18164727-Models, Molecular,
pubmed-meshheading:18164727-Molecular Sequence Data,
pubmed-meshheading:18164727-Periplasm,
pubmed-meshheading:18164727-Protein Binding,
pubmed-meshheading:18164727-Protein Folding,
pubmed-meshheading:18164727-Protein Structure, Secondary,
pubmed-meshheading:18164727-Protein Structure, Tertiary,
pubmed-meshheading:18164727-Sequence Homology, Amino Acid,
pubmed-meshheading:18164727-Serine Endopeptidases,
pubmed-meshheading:18164727-Static Electricity,
pubmed-meshheading:18164727-Substrate Specificity,
pubmed-meshheading:18164727-Surface Properties
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| pubmed:year |
2008
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| pubmed:articleTitle |
Crystal structure of a bacterial signal Peptide peptidase.
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| pubmed:affiliation |
Department of Molecular Biology and Biochemistry, Simon Fraser University, South Science Building, 8888 University Drive, Burnaby, British Columbia, Canada.
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| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|