2WL8

X-ray crystal structure of Pex19p

Summary for 2WL8

• Entry DOI: 10.2210/pdb2wl8/pdb
• Related: 2W85
• Descriptor: PEROXISOMAL BIOGENESIS FACTOR 19 (2 entities in total)
• Functional Keywords: protein transport, biogenesis disorder, zellweger syndrome, membrane, prenylation
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 4
• Total formula weight: 57472.75

Authors

Schueller, N.,Holton, S.J.,Stanley, W.A.,Song, Y.H.,Konarev, P.,Roessle, M.,Erdmann, R.,Schliebs, W.,Wilmanns, M. (deposition date: 2009-06-22, release date: 2010-06-23, Last modification date: 2024-05-08)

Primary citation

Schueller, N.,Holton, S.J.,Fodor, K.,Milewski, M.,Konarev, P.,Stanley, W.A.,Wolf, J.,Erdmann, R.,Schliebs, W.,Song, Y.H.,Wilmanns, M.
The Peroxisomal Receptor Pex19P Forms a Helical Mpts Recognition Domain.
Embo J., 29:2491-, 2010

PubMed 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.

PubMed: 20531392
DOI: 10.1038/EMBOJ.2010.115

Experimental method

X-RAY DIFFRACTION (2.05 Å)