2C0L

TPR DOMAIN OF HUMAN PEX5P IN COMPLEX WITH HUMAN MSCP2

Summary for 2C0L

• Entry DOI: 10.2210/pdb2c0l/pdb
• Related: 1FCH 1QND
• Descriptor: PEROXISOMAL TARGETING SIGNAL 1 RECEPTOR, NONSPECIFIC LIPID-TRANSFER PROTEIN (3 entities in total)
• Functional Keywords: transport protein/receptor, tpr repeat, transport, import receptor complex, peroxisome, disease mutation, protein transport, zellweger syndrome, alternative initiation, lipid transport, lipid-binding, mitochondrion, transit peptide, transport protein-receptor complex
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 2
• Total formula weight: 46696.17

Authors

Stanley, W.A.,Kursula, P.,Wilmanns, M. (deposition date: 2005-09-05, release date: 2006-11-15, Last modification date: 2024-05-08)

Primary citation

Stanley, W.A.,Filipp, F.V.,Kursula, P.,Schuller, N.,Erdmann, R.,Schliebs, W.,Sattler, M.,Wilmanns, M.
Recognition of a Functional Peroxisome Type 1 Target by the Dynamic Import Receptor Pex5P.
Mol.Cell, 24:653-, 2006

PubMed Abstract: Peroxisomes require the translocation of folded and functional target proteins of various sizes across the peroxisomal membrane. We have investigated the structure and function of the principal import receptor Pex5p, which recognizes targets bearing a C-terminal peroxisomal targeting signal type 1. Crystal structures of the receptor in the presence and absence of a peroxisomal target, sterol carrier protein 2, reveal major structural changes from an open, snail-like conformation into a closed, circular conformation. These changes are caused by a long loop C terminal to the 7-fold tetratricopeptide repeat segments. Mutations in residues of this loop lead to defects in peroxisomal import in human fibroblasts. The structure of the receptor/cargo complex demonstrates that the primary receptor-binding site of the cargo is structurally and topologically autonomous, enabling the cargo to retain its native structure and function.

PubMed: 17157249
DOI: 10.1016/J.MOLCEL.2006.10.024

Experimental method

X-RAY DIFFRACTION (2.3 Å)