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2a40

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|PDB= 2a40 |SIZE=350|CAPTION= <scene name='initialview01'>2a40</scene>, resolution 1.80&Aring;
|PDB= 2a40 |SIZE=350|CAPTION= <scene name='initialview01'>2a40</scene>, resolution 1.80&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Deoxyribonuclease_I Deoxyribonuclease I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.1 3.1.21.1]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Deoxyribonuclease_I Deoxyribonuclease I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.1 3.1.21.1] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[2a3z|2A3Z]], [[2a41|2A41]], [[2a42|2A42]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a40 OCA], [http://www.ebi.ac.uk/pdbsum/2a40 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2a40 RCSB]</span>
}}
}}
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[[Category: Dominguez, R.]]
[[Category: Dominguez, R.]]
[[Category: Kerff, F.]]
[[Category: Kerff, F.]]
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[[Category: ATP]]
 
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[[Category: CA]]
 
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[[Category: GOL]]
 
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[[Category: MG]]
 
[[Category: actin]]
[[Category: actin]]
[[Category: arp2/3]]
[[Category: arp2/3]]
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[[Category: wh2]]
[[Category: wh2]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:34:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:47:31 2008''

Revision as of 22:47, 30 March 2008

Image:2a40.gif


PDB ID 2a40

Drag the structure with the mouse to rotate
, resolution 1.80Å
Ligands: , , , , ,
Activity: Deoxyribonuclease I, with EC number 3.1.21.1
Related: 2A3Z, 2A41, 2A42


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Ternary complex of the WH2 domain of WAVE with Actin-DNAse I


Overview

Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) is a small and widespread actin-binding motif. In the WASP family, WH2 plays a role in filament nucleation by Arp2/3 complex. Here we describe the crystal structures of complexes of actin with the WH2 domains of WASP, WASP-family verprolin homologous protein, and WASP-interacting protein. Despite low sequence identity, WH2 shares structural similarity with the N-terminal portion of the actin monomer-sequestering thymosin beta domain (Tbeta). We show that both domains inhibit nucleotide exchange by targeting the cleft between actin subdomains 1 and 3, a common binding site for many unrelated actin-binding proteins. Importantly, WH2 is significantly shorter than Tbeta but binds actin with approximately 10-fold higher affinity. WH2 lacks a C-terminal extension that in Tbeta4 becomes involved in monomer sequestration by interfering with intersubunit contacts in F-actin. Owing to their shorter length, WH2 domains connected in tandem by short linkers can coexist with intersubunit contacts in F-actin and are proposed to function in filament nucleation by lining up actin subunits along a filament strand. The WH2-central region of WASP-family proteins is proposed to function in an analogous way by forming a special class of tandem repeats whose function is to line up actin and Arp2 during Arp2/3 nucleation. The structures also suggest a mechanism for how profilin-binding Pro-rich sequences positioned N-terminal to WH2 could feed actin monomers directly to WH2, thereby playing a role in filament elongation.

About this Structure

2A40 is a Protein complex structure of sequences from Bos taurus and Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly., Chereau D, Kerff F, Graceffa P, Grabarek Z, Langsetmo K, Dominguez R, Proc Natl Acad Sci U S A. 2005 Nov 15;102(46):16644-9. Epub 2005 Nov 7. PMID:16275905

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