3vn5

Crystal structure of Aquifex aeolicus RNase H3

spinqualitylabelsall models 3vn5, resolution 1.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vn5 is a 1 chain structure with sequence from Aquifex aeolicus vf5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: aq_1768, rnhC (Aquifex aeolicus VF5) Activity: Ribonuclease H, with EC number 3.1.26.4 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed The crystal structure of ribonuclease H3 from Aquifex aeolicus (Aae-RNase H3) was determined at 2.0 A resolution. Aae-RNase H3 consists of an N-terminal TATA box-binding protein (TBP)-like domain (N-domain) and a C-terminal RNase H domain (C-domain). The structure of the C-domain highly resembles that of Bacillus stearothermophilus RNase H3 (Bst-RNase H3), except that it contains three disulfide bonds, and the fourth conserved glutamate residue of the Asp-Glu-Asp-Glu active site motif (Glu198) is located far from the active site. These disulfide bonds were shown to contribute to hyper-stabilization of the protein. Non-conserved Glu194 was identified as the fourth active site residue. The structure of the N-domain without the C-domain also highly resembles that of Bst-RNase H3. However, the arrangement of the N-domain relative to the C-domain greatly varies for these proteins because of the difference in the linker size between the domains. The linker of Bst-RNase H3 is relatively long and flexible, while that of Aae-RNase H3 is short and assumes a helix formation. Biochemical characterizations of Aae-RNase H3 and its derivatives without the N- or C-domain or with a mutation in the N-domain indicate that the N-domain of Aae-RNase H3 is important for substrate binding, and uses the flat surface of the beta-sheet for substrate binding. However, this surface is located far from the active site and on the opposite side to the active site. We propose that the N-domain of Aae-RNase H3 is required for initial contact with the substrate. The resulting complex may be rearranged such that only the C-domain forms a complex with the substrate. Structure and characterization of RNase H3 from Aquifex aeolicus.,Jongruja N, You DJ, Angkawidjaja C, Kanaya E, Koga Y, Kanaya S FEBS J. 2012 Aug;279(15):2737-53. doi: 10.1111/j.1742-4658.2012.08657.x. Epub, 2012 Jul 3. PMID:22686566 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribonuclease Temp

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