1ux4: Difference between revisions
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ux4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ux4 OCA], [http://www.ebi.ac.uk/pdbsum/1ux4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ux4 RCSB]</span> | |||
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[[Category: fh2 actin cytoskeleton]] | [[Category: fh2 actin cytoskeleton]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:16:34 2008'' | ||
Revision as of 00:16, 31 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURES OF A FORMIN HOMOLOGY-2 DOMAIN REVEAL A TETHERED-DIMER ARCHITECTURE
OverviewOverview
Formin proteins participate in a wide range of cytoskeletal processes in all eukaryotes. The defining feature of formins is a highly conserved approximately 400 residue region, the Formin Homology-2 (FH2) domain, which has recently been found to nucleate actin filaments. Here we report crystal structures of the S. cerevesiae Bni1p FH2 domain. The mostly alpha-helical FH2 domain forms a unique "tethered dimer" in which two elongated actin binding heads are tied together at either end by an unusual lasso and linker structure. Biochemical and crystallographic observations indicate that the dimer is stable but flexible, with flexibility between the two halves of the dimer conferred by the linker segments. Although each half of the dimer is competent to interact with filament ends, the intact dimer is required for actin nucleation and processive capping. The tethered dimer architecture may allow formins to stair-step on the barbed end of an elongating nascent filament.
About this StructureAbout this Structure
1UX4 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture., Xu Y, Moseley JB, Sagot I, Poy F, Pellman D, Goode BL, Eck MJ, Cell. 2004 Mar 5;116(5):711-23. PMID:15006353
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