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Title: Insights into the Influence of Nucleotides on Actin Family Proteins from Seven Structures of Arp2/3 Complex

Abstract

ATP is required for nucleation of actin filament branches by Arp2/3 complex, but the influence of ATP binding and hydrolysis are poorly understood. We determined crystal structures of bovine Arp2/3 complex cocrystalized with various bound adenine nucleotides and cations. Nucleotide binding favors closure of the nucleotide binding cleft of Arp3, but no large scale conformational changes in the complex. Thus, ATP binding does not directly activate Arp2/3 complex, but is part of a network of interactions that contribute to nucleation. We compared nucleotide-induced conformational changes of residues lining the cleft in Arp3 and actin structures to construct a movie depicting the proposed ATPase cycle for the actin family. Chemical crosslinking stabilized subdomain 1 of Arp2, revealing new electron density for 69 residues in this subdomain. Steric clashes with Arp3 appear to be responsible for intrinsic disorder of subdomains 1 and 2 of Arp2 in inactive Arp2/3 complex.

Authors:
;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
930431
Report Number(s):
BNL-81174-2008-JA
Journal ID: ISSN 1097-2765; TRN: US200904%%707
DOE Contract Number:
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Molecular Cell; Journal Volume: 26
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; ACTIN; ADENINES; CATIONS; CATTLE; CONFORMATIONAL CHANGES; CRYSTAL STRUCTURE; ELECTRON DENSITY; HYDROLYSIS; LINERS; NUCLEATION; NUCLEOTIDES; PROTEINS; RESIDUES; national synchrotron light source

Citation Formats

Nolen,B., and Pollard, T. Insights into the Influence of Nucleotides on Actin Family Proteins from Seven Structures of Arp2/3 Complex. United States: N. p., 2007. Web. doi:10.1016/j.molcel.2007.04.017.
Nolen,B., & Pollard, T. Insights into the Influence of Nucleotides on Actin Family Proteins from Seven Structures of Arp2/3 Complex. United States. doi:10.1016/j.molcel.2007.04.017.
Nolen,B., and Pollard, T. Mon . "Insights into the Influence of Nucleotides on Actin Family Proteins from Seven Structures of Arp2/3 Complex". United States. doi:10.1016/j.molcel.2007.04.017.
@article{osti_930431,
title = {Insights into the Influence of Nucleotides on Actin Family Proteins from Seven Structures of Arp2/3 Complex},
author = {Nolen,B. and Pollard, T.},
abstractNote = {ATP is required for nucleation of actin filament branches by Arp2/3 complex, but the influence of ATP binding and hydrolysis are poorly understood. We determined crystal structures of bovine Arp2/3 complex cocrystalized with various bound adenine nucleotides and cations. Nucleotide binding favors closure of the nucleotide binding cleft of Arp3, but no large scale conformational changes in the complex. Thus, ATP binding does not directly activate Arp2/3 complex, but is part of a network of interactions that contribute to nucleation. We compared nucleotide-induced conformational changes of residues lining the cleft in Arp3 and actin structures to construct a movie depicting the proposed ATPase cycle for the actin family. Chemical crosslinking stabilized subdomain 1 of Arp2, revealing new electron density for 69 residues in this subdomain. Steric clashes with Arp3 appear to be responsible for intrinsic disorder of subdomains 1 and 2 of Arp2 in inactive Arp2/3 complex.},
doi = {10.1016/j.molcel.2007.04.017},
journal = {Molecular Cell},
number = ,
volume = 26,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}