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- W2067945977 abstract "RNase-L Inhibitor, also known as ABCE1, is an ATP Binding Cassette (ABC) protein which contains only the two nucleotide binding domains (NBDs) and an iron sulfur (FeS) cluster. It was suggested to be associated with various aspects of protein synthesis, including the binding of translation initiation factors, translation release factors, export of ribosomal subunits from the nucleus and ribosome recycling. ABCE1 had been resolved by X-ray in its ADP-bound conformation only. The two NBDs possess a high structural similarity between themselves despite that they do not share the same sequence (33% identity only). Moreover, despite this structural symmetry, ABCE1 has been reported to be functionally asymmetric, where mutations in one NBD (E238Q, H269A) reduce its ATP hydrolysis by 30-50% of normal wild type activity, while the parallel mutations in the second NBD increase it by a 10-fold. Our study aims revealing the reason for this phenomena, while shedding light on the structure and mechanism of action of ABC domains. In the study presented, we differentiate ABC domains' structure according to different modes of nucleotide binding (ATP bound, ADP bound, and nucleotide free). We present the main global collective motions that occur upon the conformational change between those binding modes, and based on that, we derive an atomistic model for the closed (ATP-bound) conformation. Based on these atomistic models of the ATP and ADP bound conformations, nucleotide affinity and cooperativity effects which may influence that affinity are examined, with the goal to understand the source of the detected functional asymmetry." @default.
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- W2067945977 date "2012-01-01" @default.
- W2067945977 modified "2023-10-16" @default.
- W2067945977 title "Exploring the Mechanism and Functional (A)Symmetry of ATP Binding Cassette Domains" @default.
- W2067945977 doi "https://doi.org/10.1016/j.bpj.2011.11.2479" @default.
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