4.2 Article

Synergistic use of synchrotron radiation techniques for biological samples in solution: a case study on protein-ligand recognition by the peroxisomal import receptor Pex5p

Journal

JOURNAL OF SYNCHROTRON RADIATION
Volume 11, Issue -, Pages 490-496

Publisher

INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S090904950402504X

Keywords

SRCD; WAXS; SAXS; Pex5p; SCP2; protein structure; peroxisomal targeting; PTS1

Ask authors/readers for more resources

Circular dichroism spectropolarimetry and X-ray scattering data, obtained using synchrotron radiation, can yield information about the secondary and tertiary structure of proteins in solution. These techniques have been used to analyse the architecture and shape of a complex of two proteins in solution. The crystal structures of two separate proteins, the C-terminal domain of Pex5p and SCP2, are available but their complex has not previously been structurally characterized. Circular dichroism spectropolarimetry indicated that complex formation requires little secondary structure rearrangement. X-ray scattering data fit an elongated irregular 'shoe'-shaped particle of the complex of the two proteins, with dimensions of the order of 30 Angstrom x 40 Angstrom x 90 Angstrom. Comparison with the known crystal structures suggests that this 'shoe' shape requires a conformational change of the C-terminus of SCP2 to appropriately locate its peroxisomal targeting signal type-1 recognition motif into the binding pocket of the Pex5p receptor. Implications of the combined use of synchrotron-based circular dichroism spectropolarimetry and X-ray scattering in structural biology and proteomics are discussed.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.2
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available