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PDBsum entry 4jd2
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Structural protein
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PDB id
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4jd2
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Contents |
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398 a.a.
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377 a.a.
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342 a.a.
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283 a.a.
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170 a.a.
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166 a.a.
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139 a.a.
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138 a.a.
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PDB id:
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| Name: |
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Structural protein
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Title:
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Crystal structure of bos taurus arp2/3 complex binding with mus musculus gmf
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Structure:
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Actin-related protein 3. Chain: a. Synonym: actin-2, actin-like protein 3. Actin-related protein 2. Chain: b. Synonym: actin-like protein 2. Actin-related protein 2/3 complex subunit 1b. Chain: c. Synonym: arp2/3 complex 41 kda subunit, p41-arc.
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Source:
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Bos taurus. Bovine,cow,domestic cattle,domestic cow. Organism_taxid: 9913. Mus musculus. Mouse. Organism_taxid: 10090
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Resolution:
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3.08Å
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R-factor:
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0.211
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R-free:
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0.248
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Authors:
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B.J.Nolen,Q.Luan
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Key ref:
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Q.Luan
and
B.J.Nolen
(2013).
Structural basis for regulation of Arp2/3 complex by GMF.
Nat Struct Biol,
20,
1062-1068.
PubMed id:
DOI:
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Date:
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22-Feb-13
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Release date:
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17-Jul-13
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PROCHECK
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Headers
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References
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P61157
(ARP3_BOVIN) -
Actin-related protein 3 from Bos taurus
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Seq:
Struc:
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418 a.a.
398 a.a.
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A7MB62
(ARP2_BOVIN) -
Actin-related protein 2 from Bos taurus
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Seq:
Struc:
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394 a.a.
377 a.a.
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Q58CQ2
(ARC1B_BOVIN) -
Actin-related protein 2/3 complex subunit 1B from Bos taurus
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Seq:
Struc:
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372 a.a.
342 a.a.
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Q3MHR7
(ARPC2_BOVIN) -
Actin-related protein 2/3 complex subunit 2 from Bos taurus
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Seq:
Struc:
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300 a.a.
283 a.a.
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Q3T035
(ARPC3_BOVIN) -
Actin-related protein 2/3 complex subunit 3 from Bos taurus
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Seq:
Struc:
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178 a.a.
170 a.a.
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Q148J6
(ARPC4_BOVIN) -
Actin-related protein 2/3 complex subunit 4 from Bos taurus
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Seq:
Struc:
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168 a.a.
166 a.a.
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Enzyme class:
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Chains A, B, C, D, E, F, G, H:
E.C.?
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DOI no:
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Nat Struct Biol
20:1062-1068
(2013)
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PubMed id:
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Structural basis for regulation of Arp2/3 complex by GMF.
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Q.Luan,
B.J.Nolen.
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ABSTRACT
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The Arp2/3 complex mediates formation of complex cellular structures such as
lamellipodia by nucleating branched actin filaments. Arp2/3-complex activity is
precisely controlled by over a dozen regulators, yet the structural mechanism by
which regulators interact with the complex is unknown. GMF is a recently
discovered regulator of the Arp2/3 complex that can inhibit nucleation and
disassemble branches. We solved the structure of the 240-kDa assembly of Mus
musculus GMF and Bos taurus Arp2/3 complex and found that GMF binds the barbed
end of Arp2, overlapping with the proposed binding site of WASP-family proteins.
The structure suggests that GMF can bind branch junctions in the manner that
cofilin binds filament sides, consistent with a modified cofilin-like mechanism
for debranching by GMF. The GMF-Arp2 interface reveals how the ADF-H
actin-binding domain in GMF is exploited to specifically recognize Arp2/3
complex and not actin.
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