1lcu
From Proteopedia
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|PDB= 1lcu |SIZE=350|CAPTION= <scene name='initialview01'>1lcu</scene>, resolution 3.5Å | |PDB= 1lcu |SIZE=350|CAPTION= <scene name='initialview01'>1lcu</scene>, resolution 3.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LAR:LATRUNCULIN+A'>LAR</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lcu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lcu OCA], [http://www.ebi.ac.uk/pdbsum/1lcu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lcu RCSB]</span> | ||
}} | }} | ||
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[[Category: Vorobiev, S M.]] | [[Category: Vorobiev, S M.]] | ||
[[Category: Yarmola, E G.]] | [[Category: Yarmola, E G.]] | ||
| - | [[Category: ATP]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: LAR]] | ||
[[Category: muscle protein]] | [[Category: muscle protein]] | ||
[[Category: structural protein]] | [[Category: structural protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:01:11 2008'' |
Revision as of 19:01, 30 March 2008
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| , resolution 3.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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