1lcu
From Proteopedia
(New page: 200px<br /><applet load="1lcu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lcu, resolution 3.5Å" /> '''Polylysine Induces an...) |
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| - | [[Image:1lcu.jpg|left|200px]]<br /><applet load="1lcu" size=" | + | [[Image:1lcu.jpg|left|200px]]<br /><applet load="1lcu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lcu, resolution 3.5Å" /> | caption="1lcu, resolution 3.5Å" /> | ||
'''Polylysine Induces an Antiparallel Actin Dimer that Nucleates Filament Assembly: Crystal Structure at 3.5 A Resolution'''<br /> | '''Polylysine Induces an Antiparallel Actin Dimer that Nucleates Filament Assembly: Crystal Structure at 3.5 A Resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | An antiparallel actin dimer has been proposed to be an intermediate | + | 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== | ||
| - | 1LCU 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 CA, CL, ATP and LAR as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1LCU 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=CA:'>CA</scene>, <scene name='pdbligand=CL:'>CL</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=1LCU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Agbandje-Mckenna, M.]] | [[Category: Agbandje-Mckenna, M.]] | ||
| - | [[Category: Almo, S | + | [[Category: Almo, S C.]] |
| - | [[Category: Bubb, M | + | [[Category: Bubb, M R.]] |
| - | [[Category: Chapman, M | + | [[Category: Chapman, M S.]] |
[[Category: Govindasamy, L.]] | [[Category: Govindasamy, L.]] | ||
[[Category: Mckenna, R.]] | [[Category: Mckenna, R.]] | ||
[[Category: Somasundaram, T.]] | [[Category: Somasundaram, T.]] | ||
| - | [[Category: Vorobiev, S | + | [[Category: Vorobiev, S M.]] |
| - | [[Category: Yarmola, E | + | [[Category: Yarmola, E G.]] |
[[Category: ATP]] | [[Category: ATP]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: structural protein]] | [[Category: structural protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:43:54 2008'' |
Revision as of 11:43, 21 February 2008
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Polylysine Induces an Antiparallel Actin Dimer that Nucleates Filament Assembly: Crystal Structure at 3.5 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
1LCU 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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