2ami | pdb_00002ami

Solution Structure Of The Calcium-loaded N-Terminal Sensor Domain Of Centrin

spinqualitylabelsall models 2ami, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ami is a 1 chain structure with sequence from Chlre. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CATR_CHLRE] This calcium-binding protein is found in the basal body complexes (the functional homolog of the centrosome in animal cell). In mitotic cells it is specifically associated with the poles of the mitotic spindles at the sites of the duplicated basal body complexes. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structure of the N-terminal calcium sensor domain of centrin reveals the biochemical basis for domain-specific function.,Sheehan JH, Bunick CG, Hu H, Fagan PA, Meyn SM, Chazin WJ J Biol Chem. 2006 Feb 3;281(5):2876-81. Epub 2005 Nov 29. PMID:16317001 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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