2p9k: Difference between revisions

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[[Image:2p9k.jpg|left|200px]]


{{Structure
==Crystal structure of bovine Arp2/3 complex co-crystallized with ATP and crosslinked with glutaraldehyde==
|PDB= 2p9k |SIZE=350|CAPTION= <scene name='initialview01'>2p9k</scene>, resolution 2.590&Aring;
<StructureSection load='2p9k' size='340' side='right'caption='[[2p9k]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>
<table><tr><td colspan='2'>[[2p9k]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P9K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P9K FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.59&#8491;</td></tr>
|GENE= ACTR3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]), ARPC1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]), ARPC2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]), ARPC3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]), ARPC4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]), ARPC5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2p9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p9k OCA], [https://pdbe.org/2p9k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p9k RCSB], [https://www.ebi.ac.uk/pdbsum/2p9k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p9k ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ARPC5_BOVIN ARPC5_BOVIN] Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p9/2p9k_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2p9k ConSurf].
<div style="clear:both"></div>


'''Crystal structure of bovine Arp2/3 complex co-crystallized with ATP and crosslinked with glutaraldehyde'''
==See Also==
 
*[[Actin-related protein 3D structures|Actin-related protein 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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==
2P9K is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P9K OCA].
 
==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):449-57. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17499050 17499050]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Nolen, B J.]]
[[Category: Nolen BJ]]
[[Category: Pollard, T D.]]
[[Category: Pollard TD]]
[[Category: ATP]]
[[Category: CA]]
[[Category: actin]]
[[Category: complex]]
[[Category: wd repeat]]
 
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