 |
PDBsum entry 4lx1
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transport protein
|
PDB id
|
|
|
|
4lx1
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Transport protein
|
|
|
Title:
|
|
Crystal structure of myo5a globular tail domain
|
|
Structure:
|
|
Unconventional myosin-va. Chain: a, b. Fragment: dilute domain residues 1464-1855. Synonym: dilute myosin heavy chain, non-muscle, myosin heavy chain 12, myosin-12, myoxin. Engineered: yes
|
|
Source:
|
|
Homo sapiens. Human. Organism_taxid: 9606. Gene: myo5a, myh12. Expressed in: escherichia coli. Expression_system_taxid: 562
|
|
Resolution:
|
|
|
1.87Å
|
R-factor:
|
0.166
|
R-free:
|
0.199
|
|
|
Authors:
|
|
O.Pylypenko,W.Attanda,D.Coulibaly,C.Gauquelin,A.Houdusse
|
|
Key ref:
|
|
O.Pylypenko
et al.
(2013).
Structural basis of myosin V Rab GTPase-dependent cargo recognition.
Proc Natl Acad Sci U S A,
110,
20443-20448.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
29-Jul-13
|
Release date:
|
20-Nov-13
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
Q9Y4I1
(MYO5A_HUMAN) -
Unconventional myosin-Va from Homo sapiens
|
|
|
|
Seq:
Struc:
|
|
|
|
1855 a.a.
360 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Proc Natl Acad Sci U S A
110:20443-20448
(2013)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Structural basis of myosin V Rab GTPase-dependent cargo recognition.
|
|
O.Pylypenko,
W.Attanda,
C.Gauquelin,
M.Lahmani,
D.Coulibaly,
B.Baron,
S.Hoos,
M.A.Titus,
P.England,
A.M.Houdusse.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
Specific recognition of the cargo that molecular motors transport or tether to
cytoskeleton tracks allows them to perform precise cellular functions at
particular times and positions in cells. However, very little is known about how
evolution has favored conservation of functions for some isoforms, while also
allowing for the generation of new recognition sites and specialized cellular
functions. Here we present several crystal structures of the myosin Va or the
myosin Vb globular tail domain (GTD) that gives insights into how the motor is
linked to the recycling membrane compartments via Rab11 or to the melanosome
membrane via recognition of the melanophilin adaptor that binds to Rab27a. The
structures illustrate how the Rab11-binding site has been conserved during
evolution and how divergence at another site of the GTD allows more specific
interactions such as the specific recognition of melanophilin by the myosin Va
isoform. With atomic structural insights, these structures also show how either
the partner or the GTD structural plasticity upon association is critical for
selective recruitment of the motor.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Links
