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PDBsum entry 4lwz
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Protein transport
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PDB id
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4lwz
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Contents |
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162 a.a.
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367 a.a.
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346 a.a.
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PDB id:
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| Name: |
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Protein transport
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Title:
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Crystal structure of myo5b globular tail domain in complex with inactive rab11a
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Structure:
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Ras-related protein rab-11a. Chain: a, c. Fragment: dilute domain residues 1456-1848. Synonym: rab-11, yl8. Engineered: yes. Unconventional myosin-vb. Chain: b, d. Fragment: unp residues 1-177. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: rab11a, rab11. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: myo5b, kiaa1119. Expression_system_taxid: 562
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Resolution:
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2.55Å
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R-factor:
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0.234
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R-free:
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0.295
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Authors:
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O.Pylypenko,W.Attanda,C.Gauquelin,A.Houdusse
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Key ref:
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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:
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Date:
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29-Jul-13
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Release date:
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20-Nov-13
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PROCHECK
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Headers
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References
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P62491
(RB11A_HUMAN) -
Ras-related protein Rab-11A from Homo sapiens
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Seq:
Struc:
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216 a.a.
162 a.a.
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Enzyme class 1:
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Chains A, C:
E.C.3.6.5.2
- small monomeric GTPase.
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Reaction:
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GTP + H2O = GDP + phosphate + H+
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GTP
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+
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H2O
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=
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GDP
Bound ligand (Het Group name = )
corresponds exactly
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+
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phosphate
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+
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H(+)
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Enzyme class 2:
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Chains B, D:
E.C.?
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Proc Natl Acad Sci U S A
110:20443-20448
(2013)
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PubMed id:
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Structural basis of myosin V Rab GTPase-dependent cargo recognition.
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O.Pylypenko,
W.Attanda,
C.Gauquelin,
M.Lahmani,
D.Coulibaly,
B.Baron,
S.Hoos,
M.A.Titus,
P.England,
A.M.Houdusse.
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ABSTRACT
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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.
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Links
