Sökning: id:"swepub:oai:DiVA.org:uu-89386" >
Calcium ion exchang...
Calcium ion exchange in crystalline gelsolin
-
- Chumnarnsilpa, Sakesit, 1967- (författare)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,Robert Robinson
-
- Loonchanta, Anantasak (författare)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi
-
- Xue, Bo (författare)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi
-
visa fler...
-
- Robinson, Robert C. (författare)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi
-
Choe, Han (författare)
-
Urosev, Dunja (författare)
-
Wang, Hui (författare)
-
- Lindberg, Uno (författare)
- Karolinska Institutet
-
Burtnick, Leslie D (författare)
-
visa färre...
-
(creator_code:org_t)
- England : Academic Press, 2006
- 2006
- Engelska.
-
Ingår i: Journal of Molecular Biology. - England : Academic Press. - 0022-2836 .- 1089-8638. ; 357:3, s. 773-782
- Relaterad länk:
-
http://www.ncbi.nlm....
-
visa fler...
-
https://uu.diva-port... (primary) (Raw object)
-
http://uu.diva-porta...
-
http://www.ncbi.nlm....
-
https://urn.kb.se/re...
-
https://doi.org/10.1...
-
https://urn.kb.se/re...
-
http://kipublication...
-
visa färre...
Abstract
Ämnesord
Stäng
- Gelsolin is a calcium and pH-sensitive modulator of actin filament length. Here, we use X-ray crystallography to examine the extraction and exchange of calcium ions from their binding sites in different crystalline forms of the activated N and C-terminal halves of gelsolin, G1-G3 and G4-G6, respectively. We demonstrate that the combination of calcium and low pH activating conditions do not induce conformational changes in G4-G6 beyond those elicited by calcium alone. EGTA is able to remove calcium ions bound to the type I and type II metal ion-binding sites in G4-G6. Constrained by crystal contacts and stabilized by interdomain interaction surfaces, the gross structure of calcium-depleted G4-G6 remains that of the activated form. However, high-resolution details of changes in the ion-binding sites may represent the initial steps toward restoration of the arrangement of domains found in the calcium-free inactive form of gelsolin in solution. Furthermore, bathing crystals with the trivalent calcium ion mimic, Tb3+, results in anomalous scattering data that permit unequivocal localization of terbium ions in each of the proposed type I and type II ion-binding sites of both halves of gelsolin. In contrast to predictions based on solution studies, we find that no calcium ion is immune to exchange.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinsk bioteknologi -- Medicinsk bioteknologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Medical Biotechnology -- Medical Biotechnology (hsv//eng)
Nyckelord
- Actins/metabolism
- Calcium/chemistry/metabolism
- Calcium-Binding Proteins/chemistry/metabolism
- Crystallography
- X-Ray
- Gelsolin/chemistry/metabolism
- Predictive Value of Tests
- Protein Structure
- Tertiary
- Biochemistry
- Biokemi
- Biochemistry
- biokemi
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas