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| [[Image:2p9i.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2p9i| PDB=2p9i | SCENE= }} | | {{STRUCTURE_2p9i| PDB=2p9i | SCENE= }} |
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| '''Crystal Structure of bovine Arp2/3 Complex co-crystallized with ADP and crosslinked with gluteraldehyde'''
| | ===Crystal Structure of bovine Arp2/3 Complex co-crystallized with ADP and crosslinked with gluteraldehyde=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17499050}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17499050 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17499050}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Complex]] | | [[Category: Complex]] |
| [[Category: Wd repeat]] | | [[Category: Wd repeat]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:40:05 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:14:39 2008'' |