Crystal structure of Arp2/3 complex

R. C. Robinson; K. Turbedsky; D. A. Kaiser; J. B. Marchand; H. N. Higgs; S. Choe; T. D. Pollard

doi:10.1126/science.1066333

Crystal structure of Arp2/3 complex

R. C. Robinson, K. Turbedsky, D. A. Kaiser, J. B. Marchand, H. N. Higgs, S. Choe, T. D. Pollard

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Abstract

We determined a crystal structure of bovine Arp2/3 complex, an assembly of seven proteins that initiates actin polymerization in eukaryotic cells, at 2.0 angstrom resolution. Actin-related protein 2 (Arp2) and Arp3 are folded like actin, with distinctive surface features. Subunits ARPC2 p34 and ARPC4 p20 in the core of the complex associate through long carboxyl-.terminal α helices and have similarly folded amino-terminal α/β domains. ARPC1 p40 is a seven-blade β propeller with an insertion that may associate with the side of an actin filament. ARPC3 p21 and ARPC5 p16 are globular α-helical subunits. We predict that WASp/Scar proteins activate Arp2/3 complex by bringing Arp2 into proximity with Arp3 for nucleation of a branch on the side of a preexisting actin filament.

Original language	English
Pages (from-to)	1679-1684
Number of pages	6
Journal	Science
Volume	294
Issue number	5547
DOIs	https://doi.org/10.1126/science.1066333
Publication status	Published - Nov 23 2001
Externally published	Yes

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title = "Crystal structure of Arp2/3 complex",

abstract = "We determined a crystal structure of bovine Arp2/3 complex, an assembly of seven proteins that initiates actin polymerization in eukaryotic cells, at 2.0 angstrom resolution. Actin-related protein 2 (Arp2) and Arp3 are folded like actin, with distinctive surface features. Subunits ARPC2 p34 and ARPC4 p20 in the core of the complex associate through long carboxyl-.terminal α helices and have similarly folded amino-terminal α/β domains. ARPC1 p40 is a seven-blade β propeller with an insertion that may associate with the side of an actin filament. ARPC3 p21 and ARPC5 p16 are globular α-helical subunits. We predict that WASp/Scar proteins activate Arp2/3 complex by bringing Arp2 into proximity with Arp3 for nucleation of a branch on the side of a preexisting actin filament.",

author = "Robinson, {R. C.} and K. Turbedsky and Kaiser, {D. A.} and Marchand, {J. B.} and Higgs, {H. N.} and S. Choe and Pollard, {T. D.}",

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T1 - Crystal structure of Arp2/3 complex

AU - Robinson, R. C.

AU - Turbedsky, K.

AU - Kaiser, D. A.

AU - Marchand, J. B.

AU - Higgs, H. N.

AU - Choe, S.

AU - Pollard, T. D.

PY - 2001/11/23

Y1 - 2001/11/23

N2 - We determined a crystal structure of bovine Arp2/3 complex, an assembly of seven proteins that initiates actin polymerization in eukaryotic cells, at 2.0 angstrom resolution. Actin-related protein 2 (Arp2) and Arp3 are folded like actin, with distinctive surface features. Subunits ARPC2 p34 and ARPC4 p20 in the core of the complex associate through long carboxyl-.terminal α helices and have similarly folded amino-terminal α/β domains. ARPC1 p40 is a seven-blade β propeller with an insertion that may associate with the side of an actin filament. ARPC3 p21 and ARPC5 p16 are globular α-helical subunits. We predict that WASp/Scar proteins activate Arp2/3 complex by bringing Arp2 into proximity with Arp3 for nucleation of a branch on the side of a preexisting actin filament.

AB - We determined a crystal structure of bovine Arp2/3 complex, an assembly of seven proteins that initiates actin polymerization in eukaryotic cells, at 2.0 angstrom resolution. Actin-related protein 2 (Arp2) and Arp3 are folded like actin, with distinctive surface features. Subunits ARPC2 p34 and ARPC4 p20 in the core of the complex associate through long carboxyl-.terminal α helices and have similarly folded amino-terminal α/β domains. ARPC1 p40 is a seven-blade β propeller with an insertion that may associate with the side of an actin filament. ARPC3 p21 and ARPC5 p16 are globular α-helical subunits. We predict that WASp/Scar proteins activate Arp2/3 complex by bringing Arp2 into proximity with Arp3 for nucleation of a branch on the side of a preexisting actin filament.

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JO - Science

JF - Science

IS - 5547

ER -

Crystal structure of Arp2/3 complex

Abstract

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