1ijj

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(New page: 200px<br /><applet load="1ijj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ijj, resolution 2.85&Aring;" /> '''THE X-RAY CRYSTAL ST...)
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[[Image:1ijj.jpg|left|200px]]<br /><applet load="1ijj" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ijj.jpg|left|200px]]<br /><applet load="1ijj" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ijj, resolution 2.85&Aring;" />
caption="1ijj, resolution 2.85&Aring;" />
'''THE X-RAY CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RABBIT SKELETAL MUSCLE ACTIN AND LATRUNCULIN A AT 2.85 A RESOLUTION'''<br />
'''THE X-RAY CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RABBIT SKELETAL MUSCLE ACTIN AND LATRUNCULIN A AT 2.85 A RESOLUTION'''<br />
==Overview==
==Overview==
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An antiparallel actin dimer has been proposed to be an intermediate, species during actin filament nucleation. We now show that latrunculin A, a marine natural product that inhibits actin polymerization, arrests, polylysine-induced nucleation at the level of an antiparallel dimer, resulting in its accumulation. These dimers, when composed of, pyrene-labeled actin subunits, give rise to a fluorescent excimer, permitting detection during polymerization in vitro. We report the, crystallographic structure of the polylysine-actin-latrunculin A complex, at 3.5-A resolution. The non-crystallographic contact is consistent with a, dimeric structure and confirms the antiparallel orientation of its, subunits. The crystallographic contacts reveal that the mobile DNase I, binding loop of one subunit of a symmetry-related antiparallel actin dimer, is partially stabilized in the interface between the two subunits of a, second antiparallel dimer. These results provide a potential explanation, for the paradoxical nucleation of actin filaments that have exclusively, parallel subunits by a dimer containing antiparallel subunits.
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An antiparallel actin dimer has been proposed to be an intermediate species during actin filament nucleation. We now show that latrunculin A, a marine natural product that inhibits actin polymerization, arrests polylysine-induced nucleation at the level of an antiparallel dimer, resulting in its accumulation. These dimers, when composed of pyrene-labeled actin subunits, give rise to a fluorescent excimer, permitting detection during polymerization in vitro. We report the crystallographic structure of the polylysine-actin-latrunculin A complex at 3.5-A resolution. The non-crystallographic contact is consistent with a dimeric structure and confirms the antiparallel orientation of its subunits. The crystallographic contacts reveal that the mobile DNase I binding loop of one subunit of a symmetry-related antiparallel actin dimer is partially stabilized in the interface between the two subunits of a second antiparallel dimer. These results provide a potential explanation for the paradoxical nucleation of actin filaments that have exclusively parallel subunits by a dimer containing antiparallel subunits.
==About this Structure==
==About this Structure==
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1IJJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with MG, ATP and LAR as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IJJ OCA].
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1IJJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=LAR:'>LAR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IJJ OCA].
==Reference==
==Reference==
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[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Almo, S.C.]]
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[[Category: Almo, S C.]]
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[[Category: Bubb, M.R.]]
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[[Category: Bubb, M R.]]
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[[Category: Vorobiev, S.M.]]
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[[Category: Vorobiev, S M.]]
[[Category: ATP]]
[[Category: ATP]]
[[Category: LAR]]
[[Category: LAR]]
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[[Category: latrunculin]]
[[Category: latrunculin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:27:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:12:30 2008''

Revision as of 11:12, 21 February 2008


1ijj, resolution 2.85Å

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THE X-RAY CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RABBIT SKELETAL MUSCLE ACTIN AND LATRUNCULIN A AT 2.85 A RESOLUTION

Overview

An antiparallel actin dimer has been proposed to be an intermediate species during actin filament nucleation. We now show that latrunculin A, a marine natural product that inhibits actin polymerization, arrests polylysine-induced nucleation at the level of an antiparallel dimer, resulting in its accumulation. These dimers, when composed of pyrene-labeled actin subunits, give rise to a fluorescent excimer, permitting detection during polymerization in vitro. We report the crystallographic structure of the polylysine-actin-latrunculin A complex at 3.5-A resolution. The non-crystallographic contact is consistent with a dimeric structure and confirms the antiparallel orientation of its subunits. The crystallographic contacts reveal that the mobile DNase I binding loop of one subunit of a symmetry-related antiparallel actin dimer is partially stabilized in the interface between the two subunits of a second antiparallel dimer. These results provide a potential explanation for the paradoxical nucleation of actin filaments that have exclusively parallel subunits by a dimer containing antiparallel subunits.

About this Structure

1IJJ is a Single protein structure of sequence from Oryctolagus cuniculus with , and as ligands. Full crystallographic information is available from OCA.

Reference

Polylysine induces an antiparallel actin dimer that nucleates filament assembly: crystal structure at 3.5-A resolution., Bubb MR, Govindasamy L, Yarmola EG, Vorobiev SM, Almo SC, Somasundaram T, Chapman MS, Agbandje-McKenna M, McKenna R, J Biol Chem. 2002 Jun 7;277(23):20999-1006. Epub 2002 Apr 3. PMID:11932258

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