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PDBsum entry 3mkq
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Transport protein
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PDB id
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3mkq
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Contents |
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* Residue conservation analysis
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PDB id:
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Transport protein
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Title:
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Crystal structure of yeast alpha/betaprime-cop subcomplex of the copi vesicular coat
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Structure:
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Coatomer beta'-subunit. Chain: a, c, e. Fragment: unp residues 1-814. Engineered: yes. Coatomer subunit alpha. Chain: b, d, f. Fragment: unp residues 642-818. Synonym: alpha-coat protein, alpha-cop. Engineered: yes
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 307796. Strain: yjm789. Gene: sec27, scy_1929. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Brewer's yeast,lager beer yeast,yeast. Organism_taxid: 4932.
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Resolution:
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2.50Å
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R-factor:
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0.221
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R-free:
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0.272
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Authors:
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C.Lee,J.Goldberg
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Key ref:
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C.Lee
and
J.Goldberg
(2010).
Structure of coatomer cage proteins and the relationship among COPI, COPII, and clathrin vesicle coats.
Cell,
142,
123-132.
PubMed id:
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Date:
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15-Apr-10
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Release date:
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14-Jul-10
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PROCHECK
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Headers
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References
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Enzyme class:
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Chains A, B, C, D, E, F:
E.C.?
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Cell
142:123-132
(2010)
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PubMed id:
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Structure of coatomer cage proteins and the relationship among COPI, COPII, and clathrin vesicle coats.
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C.Lee,
J.Goldberg.
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ABSTRACT
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COPI-coated vesicles form at the Golgi apparatus from two cytosolic components,
ARF G protein and coatomer, a heptameric complex that can polymerize into a cage
to deform the membrane into a bud. Although coatomer shares a common
evolutionary origin with COPII and clathrin vesicle coat proteins, the
architectural relationship among the three cages is unclear. Strikingly, the
alphabeta'-COP core of coatomer crystallizes as a triskelion in which three
copies of a beta'-COP beta-propeller domain converge through their axial ends.
We infer that the trimer constitutes the vertex of the COPI cage. Our model
proposes that the COPI cage is intermediate in design between COPII and
clathrin: COPI shares with clathrin an arrangement of three curved
alpha-solenoid legs radiating from a common center, and COPI shares with COPII
highly similar vertex interactions involving the axial ends of beta-propeller
domains.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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C.K.Yip,
and
T.Walz
(2011).
Molecular structure and flexibility of the yeast coatomer as revealed by electron microscopy.
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J Mol Biol,
408,
825-831.
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P.Mill,
P.J.Lockhart,
E.Fitzpatrick,
H.S.Mountford,
E.A.Hall,
M.A.Reijns,
M.Keighren,
M.Bahlo,
C.J.Bromhead,
P.Budd,
S.Aftimos,
M.B.Delatycki,
R.Savarirayan,
I.J.Jackson,
and
D.J.Amor
(2011).
Human and mouse mutations in WDR35 cause short-rib polydactyly syndromes due to abnormal ciliogenesis.
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Am J Hum Genet,
88,
508-515.
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J.E.Rothman,
and
J.E.Rothman
(2010).
The future of Golgi research.
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Mol Biol Cell,
21,
3776-3780.
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J.H.Hurley,
E.Boura,
L.A.Carlson,
and
B.Różycki
(2010).
Membrane budding.
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Cell,
143,
875-887.
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K.E.Routledge,
V.Gupta,
and
W.E.Balch
(2010).
Emergent properties of proteostasis-COPII coupled systems in human health and disease.
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Mol Membr Biol,
27,
385-397.
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M.Pinot,
B.Goud,
and
J.B.Manneville
(2010).
Physical aspects of COPI vesicle formation.
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Mol Membr Biol,
27,
428-442.
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S.C.Harrison,
and
T.Kirchhausen
(2010).
Structural biology: Conservation in vesicle coats.
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Nature,
466,
1048-1049.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
