3byh: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= PS1TP5BP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= PS1TP5BP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3byh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3byh OCA], [http://www.ebi.ac.uk/pdbsum/3byh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3byh RCSB]</span> | |||
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[[Category: structural protein]] | [[Category: structural protein]] | ||
''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 05:29:42 2008'' | ||
Revision as of 05:29, 31 March 2008
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| Gene: | PS1TP5BP1 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Model of actin-fimbrin ABD2 complex
OverviewOverview
Many actin binding proteins have a modular architecture, and calponin-homology (CH) domains are one such structurally conserved module found in numerous proteins that interact with F-actin. The manner in which CH-domains bind F-actin has been controversial. Using cryo-EM and a single-particle approach to helical reconstruction, we have generated 12-A-resolution maps of F-actin alone and F-actin decorated with a fragment of human fimbrin (L-plastin) containing tandem CH-domains. The high resolution allows an unambiguous fit of the crystal structure of fimbrin into the map. The interaction between fimbrin ABD2 (actin binding domain 2) and F-actin is different from any interaction previously observed or proposed for tandem CH-domain proteins, showing that the structural conservation of the CH-domains does not lead to a conserved mode of interaction with F-actin. Both the stapling of adjacent actin protomers and the additional closure of the nucleotide binding cleft in F-actin when the fimbrin fragment binds may explain how fimbrin can stabilize actin filaments. A mechanism is proposed where ABD1 of fimbrin becomes activated for binding a second actin filament after ABD2 is bound to a first filament, and this can explain how mutations of residues buried in the interface between ABD2 and ABD1 can rescue temperature-sensitive defects in actin.
About this StructureAbout this Structure
3BYH is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
High-resolution cryo-EM structure of the F-actin-fimbrin/plastin ABD2 complex., Galkin VE, Orlova A, Cherepanova O, Lebart MC, Egelman EH, Proc Natl Acad Sci U S A. 2008 Feb 5;105(5):1494-8. Epub 2008 Jan 30. PMID:18234857
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