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The crystal structu...
The crystal structure of the C-terminus of adseverin: Implications for actin binding
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- Chumnarnsilpa, Sakesit, 1967- (författare)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,Robert Robinson
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- Ma, Qing (författare)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi
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- Lin Lee, Wei (författare)
- Institute of Molecular and Cell Biology, A*STAR, Singapore
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- Burtnick, Leslie D. (författare)
- epartment of Chemistry and Centre for Blood Research, Life Sciences Institute, The University of British Columbia, Canada
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- Robinson, Robert C. (författare)
- Institute of Molecular and Cell Biology, A*STAR, Singapore
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(creator_code:org_t)
- Engelska.
- Relaterad länk:
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https://urn.kb.se/re...
Abstract
Ämnesord
Stäng
- Adseverin is a member of the calcium-regulated gelsolin superfamily of actin severing and capping proteins. Adseverin comprises six homologous domains (A1-A6) which share 60% homology with the six domains from gelsolin (G1-G6). Adseverin is truncated in comparison to gelsolin, lacking the C-terminal extension which masks the F-actin binding site in calcium-free gelsolin. Biochemical assays have indicated differences in the interaction of the C-terminus halves of adseverin and gelsolin with actin. Gelsolin contacts actin through a major site on G4 and a minor site on G6, while adseverin uses a site on A5. Here we present the X-ray structure of the activated C-terminal half of adseverin (A4-A6). This structure is highly similar to that of the activated form of the C-terminal half of gelsolin (G4-G6), both in arrangement of domains and in the three bound calcium ions. Comparative analysis of the actin-binding surfaces observed in the G4-G6/actin structure suggests that adseverin in this conformation will also be able to interact with actin through A4 and A6, while the A5 surface is obscured. A model of calcium-free adseverin constructed from the structure of gelsolin predicts that the interaction between A2 and A6 provides sterric inhibition to prevent interaction with F-actin in the absence of calcium. Actin-binding assays reveal that the minimal stoichiometry of adseverin to calcium needed to disassemble actin filaments is 1:1 as compared to the 1:2 that was previously observed for gelsolin. We propose that the absence of a gelsolin-like C-terminal extension in adseverin reduces the calcium requirement for activation.
Ämnesord
- NATURVETENSKAP -- Biologi -- Strukturbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Structural Biology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- gelsolin superfamily proteins
- gelsolin
- adseverin scinderin
- actin
- calcium
- calcium-activation
- Structural biology
- Strukturbiologi
- Biochemistry
- Biokemi
- biokemi
- Biochemistry
Publikations- och innehållstyp
- pop (ämneskategori)
- ovr (ämneskategori)