2a42

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(New page: 200px<br /><applet load="2a42" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a42, resolution 1.85&Aring;" /> '''Actin-DNAse I Comple...)
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'''Actin-DNAse I Complex'''<br />
'''Actin-DNAse I Complex'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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2A42 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with CA, MG, ATP and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A42 OCA].
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2A42 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A42 OCA].
==Reference==
==Reference==
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[[Category: dnase i]]
[[Category: dnase i]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:54:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:23:23 2008''

Revision as of 14:23, 21 February 2008

Image:2a42.gif

2a42, resolution 1.85Å

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Actin-DNAse I Complex

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

2A42 is a Protein complex structure of sequences from Bos taurus and Oryctolagus cuniculus with , , and as ligands. Active as Deoxyribonuclease I, with EC number 3.1.21.1 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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