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PDBsum entry 5a1u
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Transport protein
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PDB id
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5a1u
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Contents |
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159 a.a.
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813 a.a.
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803 a.a.
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824 a.a.
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139 a.a.
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813 a.a.
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135 a.a.
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PDB id:
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| Name: |
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Transport protein
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Title:
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The structure of the copi coat triad
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Structure:
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Adp-ribosylation factor 1. Chain: a, b. Engineered: yes. Coatomer subunit alpha. Chain: c. Synonym: alpha-coat protein, alpha-cop, xenopsin-related peptide, co at protein 1. Engineered: yes. Coatomer subunit beta'.
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562. Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: spodoptera frugiperda.
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Authors:
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S.O.Dodonova,P.Diestelkoetter-Bachert,A.Von Appen,W.J.H.Hagen,R.Beck, M.Beck,F.Wieland,J.A.G.Briggs
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Key ref:
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S.O.Dodonova
et al.
(2015).
VESICULAR TRANSPORT. A structure of the COPI coat and the role of coat proteins in membrane vesicle assembly.
Science,
349,
195-198.
PubMed id:
DOI:
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Date:
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06-May-15
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Release date:
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08-Jul-15
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PROCHECK
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Headers
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References
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P11076
(ARF1_YEAST) -
ADP-ribosylation factor 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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181 a.a.
159 a.a.
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Q8CIE6
(COPA_MOUSE) -
Coatomer subunit alpha from Mus musculus
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Seq:
Struc:
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1224 a.a.
813 a.a.
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O55029
(COPB2_MOUSE) -
Coatomer subunit beta' from Mus musculus
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Seq:
Struc:
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905 a.a.
803 a.a.
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Q9QZE5
(COPG1_MOUSE) -
Coatomer subunit gamma-1 from Mus musculus
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Seq:
Struc:
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874 a.a.
824 a.a.
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P61924
(COPZ1_MOUSE) -
Coatomer subunit zeta-1 from Mus musculus
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Seq:
Struc:
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177 a.a.
139 a.a.
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Enzyme class:
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Chains A, B:
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
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+
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phosphate
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+
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H(+)
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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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Science
349:195-198
(2015)
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PubMed id:
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VESICULAR TRANSPORT. A structure of the COPI coat and the role of coat proteins in membrane vesicle assembly.
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S.O.Dodonova,
P.Diestelkoetter-Bachert,
A.von Appen,
W.J.Hagen,
R.Beck,
M.Beck,
F.Wieland,
J.A.Briggs.
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ABSTRACT
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Transport of material within cells is mediated by trafficking vesicles that bud
from one cellular compartment and fuse with another. Formation of a trafficking
vesicle is driven by membrane coats that localize cargo and polymerize into
cages to bend the membrane. Although extensive structural information is
available for components of these coats, the heterogeneity of trafficking
vesicles has prevented an understanding of how complete membrane coats assemble
on the membrane. We combined cryo-electron tomography, subtomogram averaging,
and cross-linking mass spectrometry to derive a complete model of the assembled
coat protein complex I (COPI) coat involved in traffic between the Golgi and the
endoplasmic reticulum. The highly interconnected COPI coat structure
contradicted the current "adaptor-and-cage" understanding of coated
vesicle formation.
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