3byh
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:3byh.jpg|left|200px]] | [[Image:3byh.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_3byh", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_3byh| PDB=3byh | SCENE= }} | |
| - | + | ||
| - | | | + | |
| - | }} | + | |
'''Model of actin-fimbrin ABD2 complex''' | '''Model of actin-fimbrin ABD2 complex''' | ||
| Line 30: | Line 27: | ||
[[Category: Lebart, M C.]] | [[Category: Lebart, M C.]] | ||
[[Category: Orlova, A.]] | [[Category: Orlova, A.]] | ||
| - | [[Category: | + | [[Category: Acetylation]] |
| - | [[Category: | + | [[Category: Atp-binding]] |
| - | [[Category: | + | [[Category: Cytoplasm]] |
| - | [[Category: | + | [[Category: Cytoskeleton]] |
| - | [[Category: | + | [[Category: Helical filament]] |
| - | [[Category: | + | [[Category: Methylation]] |
| - | [[Category: | + | [[Category: Nucleotide-binding]] |
| - | [[Category: | + | [[Category: Phosphoprotein]] |
| - | [[Category: | + | [[Category: Protein polymer]] |
| - | [[Category: | + | [[Category: Structural protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 21:12:23 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 18:12, 4 May 2008
Model of actin-fimbrin ABD2 complex
Overview
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 Structure
3BYH is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sun May 4 21:12:23 2008
