1FCH

CRYSTAL STRUCTURE OF THE PTS1 COMPLEXED TO THE TPR REGION OF HUMAN PEX5

Summary for 1FCH

• Entry DOI: 10.2210/pdb1fch/pdb
• Descriptor: PEROXISOMAL TARGETING SIGNAL 1 RECEPTOR, PTS1-CONTAINING PEPTIDE (3 entities in total)
• Functional Keywords: protein-peptide complex, tetratricopeptide repeat, tpr, helical repeat, signaling protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 83257.29

Authors

Gatto Jr., G.J.,Geisbrecht, B.V.,Gould, S.J.,Berg, J.M. (deposition date: 2000-07-18, release date: 2000-12-06, Last modification date: 2024-02-07)

Primary citation

Gatto Jr., G.J.,Geisbrecht, B.V.,Gould, S.J.,Berg, J.M.
Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5.
Nat.Struct.Biol., 7:1091-1095, 2000

PubMed Abstract: Many proteins contain targeting signals within their sequences that specify their delivery to particular organelles. The peroxisomal targeting signal-1 (PTS1) is a C-terminal tripeptide that is sufficient to direct proteins into peroxisomes. The PTS1 sequence closely approximates Ser-Lys-Leu-COO-. PEX5, the receptor for PTS1, interacts with the signal via a series of tetratricopeptide repeats (TPRs) within its C-terminal half. Here we report the crystal structure of a fragment of human PEX5 that includes all seven predicted TPR motifs in complex with a pentapeptide containing a PTS1 sequence. Two clusters of three TPRs almost completely surround the peptide, while a hinge region, previously identified as TPR4, forms a distinct structure that enables the two sets of TPRs to form a single binding site. This structure reveals the molecular basis for PTS1 recognition and demonstrates a novel mode of TPR-peptide interaction.

PubMed: 11101887
DOI: 10.1038/81930

Experimental method

X-RAY DIFFRACTION (2.2 Å)