Structure of the N-terminal Calcium Sensor Domain of Centrin Reveals the Biochemical Basis for Domain-specific Function.
From: Department of Biochemistry, Vanderbilt University, Nashville, Tennessee 37232-8725, USA.
The Journal of biological chemistry
- Publish Date: Feb 2006
- ISSN: 0021-9258
- Volume: 281
- Issue: 5
- Pages: 2876-81
- Medium: Print
- Language: English
- Citation (JAMA): Sheehan Jonathan H, Bunick Christopher G, Hu Haitao, et al. Structure of the N-terminal Calcium Sensor Domain of Centrin Reveals the Biochemical Basis for Domain-specific Function.. J. Biol. Chem. Feb 2006;281:2876-81
Abstract
Centrin is an essential component of microtubule-organizing centers in organisms ranging from algae and yeast to humans. It is an EF-hand calcium-binding protein with homology to calmodulin but distinct calcium binding properties. In a previously proposed model, the C-terminal domain of centrin serves as a constitutive anchor to target proteins, and the N-terminal domain serves as the sensor of calcium signals. The three-dimensional structure of the N-terminal domain of Chlamydomonas rheinhardtii centrin has been determined in the presence of calcium by solution NMR spectroscopy. The domain is found to occupy an open conformation typical of EF-hand calcium sensors. Comparison of the N- and C-terminal domains of centrin reveals a structural and biochemical basis for the domain specificity of interactions with its cellular targets and the distinct nature of centrin relative to other EF-hand proteins. An NMR titration of the centrin N-terminal domain with a fragment of the known centrin target Sfi1 reveals binding of the peptide to a discrete site on the protein, which supports the proposal that the N-terminal domain serves as a calcium sensor in centrin.
Mesh Headings (Keywords): Animals, Binding Sites, Calcium Signaling, Calcium-Binding Proteins, Chlamydomonas reinhardtii, Chromosomal Proteins, Non-Histone, EF Hand Motifs, Magnetic Resonance Spectroscopy, Protein Conformation, Solutions, Titrimetry
Check for Full Text / PubMed Unique Identifier (PMID): 16317001
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