Article
Agriculture, Multidisciplinary
Yi-Yu Chen, Meng-Si Li, Xiao Yun, Fei Xia, Meng-Jun Hu, Tengchuan Jin, Min-Jie Cao, Dong Lai, Guixia Chen, Guang-Ming Liu
Summary: Site-directed mutations were utilized to reduce the immunoreactivity of sarcoplasmic calcium-binding protein (SCP) by replacing key amino acids in conformational epitopes and calcium-binding sites. The mutant SCPs effectively inhibited the binding with wild-type SCP and downregulated the expression levels of CD63 and CD203c on basophil surface, indicating impaired calcium binding ability and reduced immunoreactivities. This approach showed potential for application in reducing immunoreactivities of other shellfish allergens.
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
(2021)
Article
Biochemistry & Molecular Biology
Alisa A. Vologzhannikova, Marina P. Shevelyova, Alexey S. Kazakov, Andrey S. Sokolov, Nadezhda Borisova, Eugene A. Permyakov, Nikoleta Kircheva, Valya Nikolova, Todor Dudev, Sergei E. Permyakov
Summary: The study investigated the interaction of Sr2+ with Ca2+ binding sites of a canonical EF-hand protein, alpha-parvalbumin, suggesting that Sr2+ and Ca2+ bind to CD/EF sites of alpha-PA with sequential binding processes. Despite lower affinity to Sr2+, alpha-PA competes with Ca2+ for the same EF-hands, inducing similar structural rearrangements. The presence of a secondary Sr2+ binding site(s) may contribute to Sr2+ impact on the functional activity of proteins.
Review
Biochemistry & Molecular Biology
Marco Pedretti, Luca Bombardi, Carolina Conter, Filippo Favretto, Paola Dominici, Alessandra Astegno
Summary: Centrins are a family of small proteins containing EF hands found in all eukaryotes and often complexed with centrosome-related structures, displaying diverse cellular functions and large variance in Ca2+ sensing abilities compared to calmodulin (CaM). Current knowledge on centrins from biophysical and structural perspectives emphasizes centrin-target interactions, providing insight into their different functions and contribution to the complexity of Ca2+ signaling cascade. This understanding can help clarify the functional redundancy of centrins and centrin-binding proteins.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Biochemistry & Molecular Biology
Emma L. Arevalo-Salina, Joel Osuna, Humberto Flores, Gloria Saab-Rincon
Summary: In this study, researchers investigated the behavior of Calbindin D-9k, a high-affinity modulator protein for Ca2+, and demonstrated that loop and helix II were necessary elements for the conformational change promoted by calcium. The fusion of chimeric motifs to an activity reporter gene indicated that the loop was the minimal element needed to induce a conformational change. The discrepancy between these results was discussed in terms of inter-motif interactions and the involvement of helix I in modulating Ca2+ affinity and restricting motif conformation.
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
(2021)
Article
Biochemistry & Molecular Biology
Seul Hoo Lee, Hogyun Seo, Hwaseok Hong, Mijeong Kim, Kyung-Jin Kim
Summary: Researchers found that IsTBP in Ideonella sakaiensis has high specificity and affinity for TPA, which helps in the degradation of PET plastic. They also developed an IsTBP variant with enhanced sensitivity, which can be used as a biosensor for PET degradation.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2023)
Article
Parasitology
Muhammad Ehsan, Rui-Si Hu, Jun-Ling Hou, Hany M. Elsheikha, Xiao-Dong Li, Pan-Hong Liang, Xing-Quan Zhu
Summary: The study demonstrates the immunomodulatory effects of a recombinant tegumental calcium-binding EF-hand protein 4 of F. gigantica (rFg-CaBP4) on goat monocytes through various experiments, showing an increase in cytokine transcription levels and major histocompatibility complex (MHC) class-II molecule expression. This sheds light on the roles of calcium-binding EF-hand proteins in host-parasite interaction and the strategies used by F. gigantica to evade host immune responses.
PARASITES & VECTORS
(2021)
Article
Chemistry, Multidisciplinary
Niels Karschin, Stefan Becker, Christian Griesinger
Summary: This study presents a new approach using pseudocontact shifts and residual dipolar couplings to study protein interdomain motion. By sampling the conformational space and using a genetic algorithm, an accurate and reproducible model of the interdomain motion of Calmodulin/Munc13-1 was obtained without prior knowledge from crystallography.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2022)
Article
Plant Sciences
Marcelo Daniel Sciorra, Elisa Fantino, Cecilia Eugenia Maria Grossi, Rita Maria Ulloa
Summary: Four members of the potato calcium-dependent protein kinase (CDPK) family exhibit structural and functional differences, with distinct expressions patterns regulated by various biotic stresses.
PLANT PHYSIOLOGY AND BIOCHEMISTRY
(2021)
Article
Immunology
Kanhu Charan Das, Ruchishree Konhar, Devendra Kumar Biswal
Summary: Continuous efforts have been made to develop candidate vaccines for tropical fascioliasis in livestock. The study aimed to create a multi-epitope subunit vaccine using calcium-binding proteins from F. gigantica. The vaccine construct was tested for its antigenicity, allergenicity, and physiochemical properties, and docked with toll-like receptor 2 for stability and interaction analysis. The research has implications for F. hepatica as well.
Article
Cell Biology
Noopur Dave, Kaice LaFavers, Gustavo Arrizabalaga
Summary: Calcium signaling plays a crucial role in the regulation of the obligate intracellular parasite Toxoplasma gondii, and a novel EF-hand domain-containing protein, TgEFP1, has been identified in this calcium homeostasis network, localizing to the PLV/ELC and PV. Knockout of TgEFP1 results in faster parasite propagation, hypersensitivity to calcium ionophore-induced egress, and premature natural egress.
Article
Biology
Eider Nunez, Frederick Jones, Arantza Muguruza-Montero, Janire Urrutia, Alejandra Aguado, Covadonga Malo, Ganeko Bernardo-Seisdedos, Carmen Domene, Oscar Millet, Nikita Gamper, Alvaro Villarroel, Henry M. Colecraft
Summary: Neuronal K(V)7 channels are highly sensitive to reactive oxygen species, and the S2S3 linker of the voltage sensor plays a crucial role in redox modulation of the channels. Recent structural studies have revealed interactions between this linker and the Ca2+-binding loop of calmodulin, specifically the EF3 hand, which is essential for the signaling. Disrupting Ca2+ binding to EF3 abolishes the oxidation-induced enhancement of K(V)7.4 currents. Furthermore, the loading of EF3 with Ca2+ is critical for the reorientation of the AB fork, which translates the Ca2+ signals.
Article
Chemistry, Physical
Netanel Mendelman, Eva Menpvitch
Summary: The study analyzed NMR relaxation from the protein S100A1 using the SRLS approach and found that calcium binding significantly alters the dynamic structure of the protein, providing new insights into the calcium-binding process. The findings show physically relevant structural, kinetic, geometric, and binding information free from deficiencies found in previous analyses using the EMF method.
JOURNAL OF PHYSICAL CHEMISTRY B
(2021)
Article
Chemistry, Multidisciplinary
Sang A. Mun, Jongseo Park, Jung Youn Kang, Taein Park, Minwoo Jin, Jihyeong Yang, Soo Hyun Eom
Summary: EF-hand proteins containing a Ca2+-binding motif are involved in cellular regulation. In addition to Ca2+, these proteins can also interact with other metals such as Mg2+, Pb2+, and Zn2+. EFhd1 and EFhd2 are actin-binding proteins that modulate actin rearrangement through Ca2+-dependent and Ca2+-independent mechanisms. This study shows that the actin-related activities of EFhd1 and EFhd2 may also be regulated by Zn2+ through coordination within their EF-hands.
Article
Biochemistry & Molecular Biology
Mohit Mazumder, Sanjeev Kumar, Devbrat Kumar, Alok Bhattacharya, S. Gourinath
Summary: Ca2+-binding proteins are found in almost all living organisms, and different types have varying affinities for calcium binding. This study introduces two new scoring schemes to estimate and manipulate calcium binding affinities in proteins containing EF hand motifs. By altering five residues, the researchers designed a unique EF-hand loop that binds calcium with high affinity. The mutant protein showed a 600-fold increase in affinity for Ca2+ compared to the wildtype protein.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2023)
Article
Biochemistry & Molecular Biology
Kenji Okumura, Yukie Maruyama, Ryuichi Takase, Bunzo Mikami, Kousaku Murata, Wataru Hashimoto
Summary: The calcium binding EF-hand-like motif in AlgQ2 of Gram-negative Sphingomonas sp. A1 stabilizes the substrate-unbound AlgQ2, but is not required for the complexation of substrate-bound AlgQ2 and AlgM1M2SS.
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
(2021)