The unusual extended C-terminal helix of the peroxisomal alpha/beta-hydrolase Lpx1 is involved in dimer contacts but dispensable for dimerization
Thoms S, Hofhuis J, Thöing C, Gartner J, Niemann H (2011)
Journal of Structural Biology 175(3): 362-371.
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Abstract / Bemerkung
The yeast peroxisomal hydrolase Lpx1 belongs to the alpha/beta-hydrolase superfamily. In the absence of Lpx1, yeast peroxisomes show an aberrant vacuolated morphology similar to what is found in peroxisomal disorder patients. Here, we present the crystal structure of Lpx1 determined at a resolution of 1.9A. The structure reveals the complete catalytic triad with an unusual location of the acid residue after strand beta6 of the canonical alpha/beta-hydrolase fold. A four-helix cap domain covers the active site. The interface between the alpha/beta-hydrolase core and the cap domain forms the potential substrate binding site, which may also comprise the tunnel that leads into the protein interior and widens into a cavity. Two further tunnels connect the active site to the protein surface, potentially facilitating substrate access. Lpx1 is a homodimer. The alpha/beta-hydrolase core folds of the two protomers form the dimer contact site. Further dimerization contacts arise from the mutual embracement of the cap domain of one protomer by the non-canonical C-terminal helix of the other, resulting in a total buried surface area of some 6000A(2). The unusual C-terminal helix sticks out from the core fold to which it is connected by an extended flexible loop. We analyzed whether this helix is required for dimerization and for import of the dimer into peroxisomes using biochemical assays in vitro and a microscopy-based interaction assay in mammalian cells. Surprisingly, the C-terminal helix is dispensable for dimerization and dimer import. The unusually robust self-interaction suggests that Lpx1 is imported into peroxisomes as dimer. Copyright 2011 Elsevier Inc. All rights reserved.
Erscheinungsjahr
2011
Zeitschriftentitel
Journal of Structural Biology
Band
175
Ausgabe
3
Seite(n)
362-371
ISSN
1047-8477
Page URI
https://pub.uni-bielefeld.de/record/2317316
Zitieren
Thoms S, Hofhuis J, Thöing C, Gartner J, Niemann H. The unusual extended C-terminal helix of the peroxisomal alpha/beta-hydrolase Lpx1 is involved in dimer contacts but dispensable for dimerization. Journal of Structural Biology. 2011;175(3):362-371.
Thoms, S., Hofhuis, J., Thöing, C., Gartner, J., & Niemann, H. (2011). The unusual extended C-terminal helix of the peroxisomal alpha/beta-hydrolase Lpx1 is involved in dimer contacts but dispensable for dimerization. Journal of Structural Biology, 175(3), 362-371. https://doi.org/10.1016/j.jsb.2011.06.008
Thoms, Sven, Hofhuis, Julia, Thöing, Christian, Gartner, Jutta, and Niemann, Hartmut. 2011. “The unusual extended C-terminal helix of the peroxisomal alpha/beta-hydrolase Lpx1 is involved in dimer contacts but dispensable for dimerization”. Journal of Structural Biology 175 (3): 362-371.
Thoms, S., Hofhuis, J., Thöing, C., Gartner, J., and Niemann, H. (2011). The unusual extended C-terminal helix of the peroxisomal alpha/beta-hydrolase Lpx1 is involved in dimer contacts but dispensable for dimerization. Journal of Structural Biology 175, 362-371.
Thoms, S., et al., 2011. The unusual extended C-terminal helix of the peroxisomal alpha/beta-hydrolase Lpx1 is involved in dimer contacts but dispensable for dimerization. Journal of Structural Biology, 175(3), p 362-371.
S. Thoms, et al., “The unusual extended C-terminal helix of the peroxisomal alpha/beta-hydrolase Lpx1 is involved in dimer contacts but dispensable for dimerization”, Journal of Structural Biology, vol. 175, 2011, pp. 362-371.
Thoms, S., Hofhuis, J., Thöing, C., Gartner, J., Niemann, H.: The unusual extended C-terminal helix of the peroxisomal alpha/beta-hydrolase Lpx1 is involved in dimer contacts but dispensable for dimerization. Journal of Structural Biology. 175, 362-371 (2011).
Thoms, Sven, Hofhuis, Julia, Thöing, Christian, Gartner, Jutta, and Niemann, Hartmut. “The unusual extended C-terminal helix of the peroxisomal alpha/beta-hydrolase Lpx1 is involved in dimer contacts but dispensable for dimerization”. Journal of Structural Biology 175.3 (2011): 362-371.
Daten bereitgestellt von European Bioinformatics Institute (EBI)
UNIPROT
2 Einträge gefunden, die diesen Artikel zitieren
Peroxisomal membrane protein LPX1 (UNIPROT: Q12405)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Download in FASTA format
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Download in FASTA format
Peroxisomal membrane protein LPX1 (UNIPROT: Q12405)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Download in FASTA format
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Download in FASTA format
PDB
2 Einträge gefunden, die diesen Artikel zitieren
x-ray diffraction (PDB: 2y6u)
Protein structure name: peroxisomal alpha-beta-hydrolase lpx1 (yor084w) from saccharomyces cerevisiae (crystal form ii)
Public wwPDB file in PDB format
Protein structure name: peroxisomal alpha-beta-hydrolase lpx1 (yor084w) from saccharomyces cerevisiae (crystal form ii)
Public wwPDB file in PDB format
x-ray diffraction (PDB: 2y6v)
Protein structure name: peroxisomal alpha-beta hydrolase lpx1 (yor084w) from saccharomyces cerevisiae (crystal form i)
Public wwPDB file in PDB format
Protein structure name: peroxisomal alpha-beta hydrolase lpx1 (yor084w) from saccharomyces cerevisiae (crystal form i)
Public wwPDB file in PDB format
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