2p9s: Difference between revisions

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==Overview==

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, cocrystallized 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.

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 cocrystallized 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.

==About this Structure==

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==Reference==

Insights into the ~~Influence~~ of ~~Nucleotides~~ on ~~Actin Family Proteins~~ from ~~Seven Structures~~ of Arp2/3 ~~Complex~~., Nolen BJ, Pollard TD, Mol Cell. 2007 May 11;26(3):449-~~457~~. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17499050 17499050]

Insights into the influence of nucleotides on actin family proteins from seven structures of Arp2/3 complex., Nolen BJ, Pollard TD, Mol Cell. 2007 May 11;26(3):449-57. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17499050 17499050]

[[Category: Bos taurus]]

[[Category: Protein complex]]

[[Category: Nolen, B.J.]]

[[Category: Nolen, B J.]]

[[Category: Pollard, T.D.]]

[[Category: Pollard, T D.]]

[[Category: ATP]]

[[Category: MG]]

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[[Category: wd repeat]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-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, cocrystallized 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.
+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 cocrystallized 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.
 ==About this Structure==
@@ Line 10: / Line 10: @@
 ==Reference==
-Insights into the Influence of Nucleotides on Actin Family Proteins from Seven Structures of Arp2/3 Complex., Nolen BJ, Pollard TD, Mol Cell. 2007 May 11;26(3):449-457. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17499050 17499050]
+Insights into the influence of nucleotides on actin family proteins from seven structures of Arp2/3 complex., Nolen BJ, Pollard TD, Mol Cell. 2007 May 11;26(3):449-57. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17499050 17499050]
 [[Category: Bos taurus]]
 [[Category: Protein complex]]
-[[Category: Nolen, B.J.]]
+[[Category: Nolen, B J.]]
-[[Category: Pollard, T.D.]]
+[[Category: Pollard, T D.]]
 [[Category: ATP]]
 [[Category: MG]]
@@ Line 21: / Line 21: @@
 [[Category: wd repeat]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:07:29 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:27:27 2008''