Structural characterization of amorphous calcium carbonate-binding protein: an insight into the mechanism of amorphous calcium carbonate formation

2013 ◽  
Vol 454 (1) ◽  
pp. 167-167 ◽  
Author(s):  
J. Su ◽  
X. Liang ◽  
Q. Zhou ◽  
G. Zhang ◽  
H. Wang ◽  
...  
Keyword(s):  
Calcium Carbonate ◽  
Structural Characterization ◽  
Binding Protein ◽  
Amorphous Calcium Carbonate ◽  
Carbonate Formation ◽  
Insight Into

Structural characterization of amorphous calcium carbonate-binding protein: an insight into the mechanism of amorphous calcium carbonate formation

2013 ◽  
Vol 453 (2) ◽  
pp. 179-186 ◽  
Author(s):  
Jingtan Su ◽  
Xiao Liang ◽  
Qiang Zhou ◽  
Guiyou Zhang ◽  
Hongzhong Wang ◽  
...  
Keyword(s):  
Calcium Carbonate ◽  
Binding Sites ◽  
Binding Protein ◽  
Homology Modelling ◽  
Size Exclusion ◽  
Structural Basis ◽  
Amorphous Calcium Carbonate ◽  
Carbonate Formation

ACC (amorphous calcium carbonate) plays an important role in biomineralization process for its function as a precursor for calcium carbonate biominerals. However, it is unclear how biomacromolecules regulate the formation of ACC precursor in vivo. In the present study, we used biochemical experiments coupled with bioinformatics approaches to explore the mechanisms of ACC formation controlled by ACCBP (ACC-binding protein). Size-exclusion chromatography, chemical cross-linking experiments and negative staining electron microscopy reveal that ACCBP is a decamer composed of two adjacent pentamers. Sequence analyses and fluorescence quenching results indicate that ACCBP contains two Ca2+-binding sites. The results of in vitro crystallization experiments suggest that one Ca2+-binding site is critical for ACC formation and the other site affects the ACC induction efficiency. Homology modelling demonstrates that the Ca2+-binding sites of pentameric ACCBP are arranged in a 5-fold symmetry, which is the structural basis for ACC formation. To the best of our knowledge, this is the first report on the structural basis for protein-induced ACC formation and it will significantly improve our understanding of the amorphous precursor pathway.

Structural Characterization of HP1264 Reveals a Novel Fold for the Flavin Mononucleotide Binding Protein

Biochemistry ◽  
2013 ◽  
Vol 52 (9) ◽  
pp. 1583-1593 ◽  
Author(s):  
Ki-Young Lee ◽  
Ji-Hun Kim ◽  
Kyu-Yeon Lee ◽  
Jiyun Lee ◽  
Ingyun Lee ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Binding Protein ◽  
Flavin Mononucleotide

Insight into the structural characterization of pure and Zr-doped hydrothermally synthesized cerium oxide nanoparticles

2019 ◽  
Vol 6 (10) ◽  
pp. 105022 ◽  
Author(s):  
Muhammad Ehsan Mazhar ◽  
Samia Bakhtawar ◽  
Anwar Manzoor Rana ◽  
Muhammad Nauman Usmani ◽  
Naeem Akhtar ◽  
...  
Keyword(s):  
Cerium Oxide ◽  
Structural Characterization ◽  
Cerium Oxide Nanoparticles ◽  
Oxide Nanoparticles ◽  
Insight Into

In vitro preparation and characterization of amorphous calcium carbonate nanoparticles for applications in curcumin delivery

2019 ◽  
Vol 54 (16) ◽  
pp. 11243-11253 ◽  
Author(s):  
Chaohui Rao ◽  
Xia Guo ◽  
Min Li ◽  
Xiaoqing Sun ◽  
Xiaojie Lian ◽  
...  
Keyword(s):  
Calcium Carbonate ◽  
Amorphous Calcium Carbonate
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