1k8k: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1k8k]] 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=1K8K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K8K FirstGlance]. <br>
<table><tr><td colspan='2'>[[1k8k]] 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=1K8K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K8K FirstGlance]. <br>
</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=1k8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k8k OCA], [https://pdbe.org/1k8k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k8k RCSB], [https://www.ebi.ac.uk/pdbsum/1k8k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k8k ProSAT]</span></td></tr>
</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&#8491;</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=1k8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k8k OCA], [https://pdbe.org/1k8k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k8k RCSB], [https://www.ebi.ac.uk/pdbsum/1k8k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k8k ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ARPC4_BOVIN ARPC4_BOVIN]] Functions as actin-binding 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. Seems to contact the mother actin filament (By similarity). [[https://www.uniprot.org/uniprot/ARPC2_BOVIN ARPC2_BOVIN]] Functions as actin-binding 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. Seems to contact the mother actin filament (By similarity). [[https://www.uniprot.org/uniprot/ARP3_BOVIN ARP3_BOVIN]] Functions as ATP-binding 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. Seems to contact the pointed end of the daughter actin filament. Plays a role in ciliogenesis (By similarity). [[https://www.uniprot.org/uniprot/ARC1B_BOVIN ARC1B_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). [[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). [[https://www.uniprot.org/uniprot/ARP2_BOVIN ARP2_BOVIN]] Functions as ATP-binding 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. Seems to contact the pointed end of the daughter actin filament. [[https://www.uniprot.org/uniprot/ARPC3_BOVIN ARPC3_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).  
[https://www.uniprot.org/uniprot/ARP3_BOVIN ARP3_BOVIN] Functions as ATP-binding 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. Seems to contact the pointed end of the daughter actin filament. Plays a role in ciliogenesis (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1k8k ConSurf].
</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=1k8k ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We determined a crystal structure of bovine Arp2/3 complex, an assembly of seven proteins that initiates actin polymerization in eukaryotic cells, at 2.0 angstrom resolution. Actin-related protein 2 (Arp2) and Arp3 are folded like actin, with distinctive surface features. Subunits ARPC2 p34 and ARPC4 p20 in the core of the complex associate through long carboxyl-terminal alpha helices and have similarly folded amino-terminal alpha/beta domains. ARPC1 p40 is a seven-blade beta propeller with an insertion that may associate with the side of an actin filament. ARPC3 p21 and ARPC5 p16 are globular alpha-helical subunits. We predict that WASp/Scar proteins activate Arp2/3 complex by bringing Arp2 into proximity with Arp3 for nucleation of a branch on the side of a preexisting actin filament.


Crystal structure of Arp2/3 complex.,Robinson RC, Turbedsky K, Kaiser DA, Marchand JB, Higgs HN, Choe S, Pollard TD Science. 2001 Nov 23;294(5547):1679-84. PMID:11721045<ref>PMID:11721045</ref>
==See Also==
 
*[[Actin-related protein 3D structures|Actin-related protein 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1k8k" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Choe, S]]
[[Category: Choe S]]
[[Category: Higgs, H N]]
[[Category: Higgs HN]]
[[Category: Kaiser, D A]]
[[Category: Kaiser DA]]
[[Category: Marchand, J B]]
[[Category: Marchand J-B]]
[[Category: Pollard, T D]]
[[Category: Pollard TD]]
[[Category: Robinson, R C]]
[[Category: Robinson RC]]
[[Category: Turbedsky, K]]
[[Category: Turbedsky K]]
[[Category: Beta-propeller]]
[[Category: Structural protein]]

Latest revision as of 07:45, 7 February 2024

Crystal Structure of Arp2/3 Complex

1k8k, resolution 2.00Å

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