3ASM

Crystal structure of Q54A mutant protein of Bst-RNase HIII

Summary for 3ASM

• Entry DOI: 10.2210/pdb3asm/pdb
• Related: 2D0A
• Descriptor: Ribonuclease HIII (2 entities in total)
• Functional Keywords: rnase, dna/rna binding, hydrolase
• Biological source: Geobacillus stearothermophilus
• Cellular location: Cytoplasm (By similarity): Q6L6Q4
• Total number of polymer chains: 1
• Total formula weight: 33815.89

Authors

Angkawidjaja, C.,Kanaya, S. (deposition date: 2010-12-16, release date: 2011-06-08, Last modification date: 2023-11-01)

Primary citation

Miyashita, S.,Tadokoro, T.,Angkawidjaja, C.,You, D.-J.,Koga, Y.,Takano, K.,Kanaya, S.
Identification of the substrate binding site in the N-terminal TBP-like domain of RNase H3.
Febs Lett., 585:2313-2317, 2011

PubMed Abstract: Ribonuclease H3 from Bacillus stearothermophilus (Bst-RNase H3) has the N-terminal TBP-like substrate-binding domain. To identify the substrate binding site in this domain, the mutant proteins of the intact protein and isolated N-domain, in which six of the seventeen residues corresponding to those involved in DNA binding of TBP are individually mutated to Ala, were constructed. All of them exhibited decreased enzymatic activities and/or substrate-binding affinities when compared to those of the parent proteins, suggesting that the N-terminal domain of RNase H3 uses the flat surface of the β-sheet for substrate binding as TBP to bind DNA. This domain may greatly change conformation upon substrate binding.

PubMed: 21664908
DOI: 10.1016/j.febslet.2011.05.064

Experimental method

X-RAY DIFFRACTION (2.603 Å)