3asm
From Proteopedia
Crystal structure of Q54A mutant protein of Bst-RNase HIII
Structural highlights
FunctionQ6L6Q4_GEOSE Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.[HAMAP-Rule:MF_00053][SAAS:SAAS00088233] Publication Abstract from PubMedRibonuclease 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 beta-sheet for substrate binding as TBP to bind DNA. This domain may greatly change conformation upon substrate binding. Identification of the substrate binding site in the N-terminal TBP-like domain of RNase H3.,Miyashita S, Tadokoro T, Angkawidjaja C, You DJ, Koga Y, Takano K, Kanaya S FEBS Lett. 2011 Jul 21;585(14):2313-7. Epub 2011 Jun 12. PMID:21664908[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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