Big Data Analytics for Earth Sciences: the EarthServer approach

Big Data Analytics is an emerging field since massive storage and computing capabilities have been made available by advanced e-infrastructures. Earth and Environmental sciences are likely to benefit from Big Data Analytics techniques supporting the processing of the large number of Earth Observation datasets currently acquired and generated through observations and simulations. However, Earth Science data and applications present specificities in terms of relevance of the geospatial information, wide heterogeneity of data models and formats, and complexity of processing. Therefore, Big Earth Data Analytics requires specifically tailored techniques and tools. The EarthServer Big Earth Data Analytics engine offers a solution for coverage-type datasets, built around a high performance array database technology, and the adoption and enhancement of standards for service interaction (OGC WCS and WCPS). The EarthServer solution, led by the collection of requirements from scientific communities and international initiatives, provides a holistic approach that ranges from query languages and scalability up to mobile access and visualization. The result is demonstrated and validated through the development of lighthouse applications in the Marine, Geology, Atmospheric, Planetary and Cryospheric science domains.

Big Data Analytics for Earth Sciences: the EarthServer approach

Big Data Analytics is an emerging field since massive storage and computing capabilities have been made available by advanced e-infrastructures. Earth and Environmental sciences are likely to benefit from Big Data Analytics techniques supporting the processing of the large number of Earth Observation datasets currently acquired and generated through observations and simulations. However, Earth Science data and applications present specificities in terms of relevance of the geospatial information, wide heterogeneity of data models and formats, and complexity of processing. Therefore, Big Earth Data Analytics requires specifically tailored techniques and tools. The EarthServer Big Earth Data Analytics engine offers a solution for coverage-type datasets, built around a high performance array database technology, and the adoption and enhancement of standards for service interaction (OGC WCS and WCPS). The EarthServer solution, led by the collection of requirements from scientific communities and international initiatives, provides a holistic approach that ranges from query languages and scalability up to mobile access and visualization. The result is demonstrated and validated through the development of lighthouse applications in the Marine, Geology, Atmospheric, Planetary and Cryospheric science domains.

Molecular mechanism of activation-triggered subunit exchange in Ca(2+)/calmodulin-dependent protein kinase II.

Activation triggers the exchange of subunits in Ca(2+)/calmodulin-dependent protein kinase II (CaMKII), an oligomeric enzyme that is critical for learning, memory, and cardiac function. The mechanism by which subunit exchange occurs remains elusive. We show that the human CaMKII holoenzyme exists in dodecameric and tetradecameric forms, and that the calmodulin (CaM)-binding element of CaMKII can bind to the hub of the holoenzyme and destabilize it to release dimers. The structures of CaMKII from two distantly diverged organisms suggest that the CaM-binding element of activated CaMKII acts as a wedge by docking at intersubunit interfaces in the hub. This converts the hub into a spiral form that can release or gain CaMKII dimers. Our data reveal a three-way competition for the CaM-binding element, whereby phosphorylation biases it towards the hub interface, away from the kinase domain and calmodulin, thus unlocking the ability of activated CaMKII holoenzymes to exchange dimers with unactivated ones.

Molecular mechanism of activation-triggered subunit exchange in Ca(2+)/calmodulin-dependent protein kinase II.

Activation triggers the exchange of subunits in Ca(2+)/calmodulin-dependent protein kinase II (CaMKII), an oligomeric enzyme that is critical for learning, memory, and cardiac function. The mechanism by which subunit exchange occurs remains elusive. We show that the human CaMKII holoenzyme exists in dodecameric and tetradecameric forms, and that the calmodulin (CaM)-binding element of CaMKII can bind to the hub of the holoenzyme and destabilize it to release dimers. The structures of CaMKII from two distantly diverged organisms suggest that the CaM-binding element of activated CaMKII acts as a wedge by docking at intersubunit interfaces in the hub. This converts the hub into a spiral form that can release or gain CaMKII dimers. Our data reveal a three-way competition for the CaM-binding element, whereby phosphorylation biases it towards the hub interface, away from the kinase domain and calmodulin, thus unlocking the ability of activated CaMKII holoenzymes to exchange dimers with unactivated ones.