Back to Search
Start Over
The peroxisomal receptor Pex19p forms a helical mPTS recognition domain.
- Source :
-
The EMBO journal [EMBO J] 2010 Aug 04; Vol. 29 (15), pp. 2491-500. Date of Electronic Publication: 2010 Jun 08. - Publication Year :
- 2010
-
Abstract
- The protein Pex19p functions as a receptor and chaperone of peroxisomal membrane proteins (PMPs). The crystal structure of the folded C-terminal part of the receptor reveals a globular domain that displays a bundle of three long helices in an antiparallel arrangement. Complementary functional experiments, using a range of truncated Pex19p constructs, show that the structured alpha-helical domain binds PMP-targeting signal (mPTS) sequences with about 10 muM affinity. Removal of a conserved N-terminal helical segment from the mPTS recognition domain impairs the ability for mPTS binding, indicating that it forms part of the mPTS-binding site. Pex19p variants with mutations in the same sequence segment abolish correct cargo import. Our data indicate a divided N-terminal and C-terminal structural arrangement in Pex19p, which is reminiscent of a similar division in the Pex5p receptor, to allow separation of cargo-targeting signal recognition and additional functions.
- Subjects :
- Amino Acid Sequence
Animals
Binding Sites
Crystallography, X-Ray
Humans
Membrane Proteins genetics
Membrane Proteins metabolism
Models, Molecular
Molecular Sequence Data
Mutation
Peroxisomes metabolism
Protein Structure, Secondary
Protein Structure, Tertiary
Sequence Alignment
Membrane Proteins chemistry
Peroxisomes chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1460-2075
- Volume :
- 29
- Issue :
- 15
- Database :
- MEDLINE
- Journal :
- The EMBO journal
- Publication Type :
- Academic Journal
- Accession number :
- 20531392
- Full Text :
- https://doi.org/10.1038/emboj.2010.115