 |
PDBsum entry 4kyo
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Transferase/transport protein
|
PDB id
|
|
|
|
4kyo
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Ligand-Induced compaction of the pex5 receptor-Binding cavity impacts protein import efficiency into peroxisomes.
|
 |
|
Authors
|
 |
K.Fodor,
J.Wolf,
K.Reglinski,
D.M.Passon,
Y.Lou,
W.Schliebs,
R.Erdmann,
M.Wilmanns.
|
 |
|
Ref.
|
 |
Traffic, 2015,
16,
85-98.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
 |
|
Abstract
|
 |
|
Peroxisomes entirely rely on the import of their proteome across the peroxisomal
membrane. Recognition efficiencies of peroxisomal proteins vary by more than
1000-fold, but the molecular rationale behind their subsequent differential
import and sorting has remained enigmatic. Using the protein cargo
alanine-glyoxylate aminotransferase as a model, an unexpected increase from 34
to 80% in peroxisomal import efficiency of a single-residue mutant has been
discovered. By high-resolution structural analysis, we found that it is the
recognition receptor PEX5 that adapts its conformation for high-affinity binding
rather than the cargo protein signal motif as previously thought. During
receptor recognition, the binding cavity of the receptor shrinks to one third of
its original volume. This process is impeded in the wild-type protein cargo
because of a bulky side chain within the recognition motif, which blocks
contraction of the PEX5 binding cavity. Our data provide a new insight into
direct protein import efficiency by removal rather than by addition of an
apparent specific sequence signature that is generally applicable to peroxisomal
matrix proteins and to other receptor recognition processes.
|
 |
|
|
|
|
 |