@article {46412,
	title = {The structure, molecular dynamics, and energetics of centrin-melittin complex.},
	journal = {Proteins},
	volume = {79},
	year = {2011},
	month = {2011 Nov},
	pages = {3132-43},
	abstract = {<p>Centrin is a calcium binding protein (CaBP) belonging to the EF-hand superfamily. As with other proteins within this family, centrin is a calcium sensor with multiple biological target proteins. We chose to study Chlamydomonas reinhardtii centrin (Crcen) and its interaction with melittin (MLT) as a model for CaBP complexes due to its amphipathic properties. Our goal was to determine the molecular interactions that lead to centrin-MLT complex formation, their relative stability, and the conformational changes associated with the interaction, when compared to the single components. For this, we determined the thermodynamic parameters that define Crcen-MLT complex formation. Two-dimensional infrared (2D IR) correlation spectroscopy were used to study the amide I{\textquoteright}, I{\textquoteright}*, and side chain bands for (13)C-Crcen, MLT, and the (13)C-Crcen-MLT complex. This approach resulted in the determination of MLT{\textquoteright}s increased helicity, while centrin was stabilized within the complex. Herein we provide the first complete molecular description of centrin-MLT complex formation and the dissociation process. Also, discussed is the first structure of a CaBP-MLT complex by X-ray crystallography, which shows that MLT has a different binding orientation than previously characterized centrin-bound peptides. Finally, all of the experimental results presented herein are consistent with centrin maintaining an extended conformation while interacting with MLT. The molecular implications of these results are: (1) the recognition of hydrophobic contacts as requirements for initial binding, (2) minimum electrostatic interactions within the C-terminal end of the peptide, and (3) van der Waals interactions within MLTs N-terminal end are required for complex formation.</p>
},
	keywords = {Calcium-Binding Proteins, Crystallography, X-Ray, Melitten, Molecular Dynamics Simulation, Protein Binding, Protein Conformation, Spectroscopy, Fourier Transform Infrared, Thermodynamics},
	issn = {1097-0134},
	doi = {10.1002/prot.23142},
	author = {Sosa, Liliana Del Valle and Alfaro, Elisa and Santiago, Jorge and Narv{\'a}ez, Daniel and Rosado, Marie Cely and Rodr{\'\i}guez, Aslin and G{\'o}mez, Ana Mar{\'\i}a and Schreiter, Eric R and Pastrana-R{\'\i}os, Belinda}
}
@article {46433,
	title = {Crystallization and preliminary X-ray characterization of full-length Chlamydomonas reinhardtii centrin.},
	journal = {Acta Crystallographica Section F Structural Biology and Crystallization Communications},
	volume = {64},
	year = {2008},
	month = {2008 May 1},
	pages = {402-4},
	abstract = {<p>Chlamydomonas reinhardtii centrin is a member of the EF-hand calcium-binding superfamily. It is found in the basal body complex and is important for flagellar motility. Like other members of the EF-hand family, centrin interacts with and modulates the function of other proteins in a calcium-dependent manner. To understand how C. reinhardtii centrin interacts with its protein targets, it has been crystallized in the presence of the model peptide melittin and X-ray diffraction data have been collected to 2.2 A resolution. The crystals are orthorhombic, with unit-cell parameters a = 52.1, b = 114.4, c = 34.8 A, and are likely to belong to space group P2(1)2(1)2.</p>
},
	keywords = {Animals, Calcium, Calcium-Binding Proteins, Chlamydomonas reinhardtii, Crystallization, Crystallography, X-Ray, Escherichia coli, Melitten, Structure-Activity Relationship},
	issn = {1744-3091},
	doi = {10.1107/S1744309108009123},
	author = {Alfaro, Elisa and Sosa, Liliana Del Valle and Sanoguet, Zuleika and Pastrana-R{\'\i}os, Belinda and Schreiter, Eric R}
}
