3byh
From Proteopedia
(New page: 200px<br /><applet load="3byh" size="350" color="white" frame="true" align="right" spinBox="true" caption="3byh" /> '''Model of actin-fimbrin ABD2 complex'''<br />...) |
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- | [[Image:3byh.jpg|left|200px]] | + | [[Image:3byh.jpg|left|200px]] |
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- | '''Model of actin-fimbrin ABD2 complex''' | + | {{Structure |
+ | |PDB= 3byh |SIZE=350|CAPTION= <scene name='initialview01'>3byh</scene> | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= PS1TP5BP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | }} | ||
+ | |||
+ | '''Model of actin-fimbrin ABD2 complex''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 3BYH is a [ | + | 3BYH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BYH OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18234857 18234857] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: structural protein]] | [[Category: structural protein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:01:45 2008'' |
Revision as of 17:01, 20 March 2008
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Gene: | PS1TP5BP1 (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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
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