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Crystal Structure Of The Catalytic Trimer Of Methanococcus Jannaschii Aspartate Transcarbamoylase, Jacqueline Vitali, Michael Colaneri Colaneri, Evan Kantrowitz
Crystal Structure Of The Catalytic Trimer Of Methanococcus Jannaschii Aspartate Transcarbamoylase, Jacqueline Vitali, Michael Colaneri Colaneri, Evan Kantrowitz
Physics Faculty Publications
The catalytic trimer of Methanococcus jannaschii aspartate transcarbamoylase is extremely heat stable, maintaining 75% of its activity after heat treatment for 60 min at 75 degrees C. We undertook its structural analysis in order to understand the molecular basis of its thermostability and gain insight on how its catalytic function adapts to high temperature. Several structural elements potentially contributing to thermostability were identified. These include: (i) changes in the amino acid composition such as a decrease in the thermolabile residues Gln and Asn, an increase in the charged residues Lys and Glu, an increase in Tyr and a decrease in …
Correlated Alternative Side Chain Conformations In The Rna-Recognition Motif Of Heterogeneous Nuclear Ribonucleoprotein A1, Jacqueline Vitali, Jianzhong Ding, Jianzhong Jiang, Ying Zhang, Adrian R. Krainer, Rui-Ming Xu
Correlated Alternative Side Chain Conformations In The Rna-Recognition Motif Of Heterogeneous Nuclear Ribonucleoprotein A1, Jacqueline Vitali, Jianzhong Ding, Jianzhong Jiang, Ying Zhang, Adrian R. Krainer, Rui-Ming Xu
Physics Faculty Publications
The RNA-recognition motif (RRM) is a common and evolutionarily conserved RNA-binding module. Crystallographic and solution structural studies have shown that RRMs adopt a compact α/β structure, in which four antiparallel β-strands form the major RNA—binding surface. Conserved aromatic residues in the RRM are located on the surface of the β-sheet and are important for RNA binding. To further our understanding of the structural basis of RRM—nucleic acid interaction, we carried out a high resolution analysis of UP1, the N-terminal, two-RRM domain of heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1), whose structure was previously solved at 1.75–1.9 Å …