3asm

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Crystal structure of Q54A mutant protein of Bst-RNase HIII

Structural highlights

3asm is a 1 chain structure with sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.603Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q6L6Q4_GEOSE Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.[HAMAP-Rule:MF_00053][SAAS:SAAS00088233]

Publication Abstract from PubMed

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 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.

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See Also

References

  1. ↑ Miyashita S, Tadokoro T, Angkawidjaja C, You DJ, Koga Y, Takano K, Kanaya S. Identification of the substrate binding site in the N-terminal TBP-like domain of RNase H3. FEBS Lett. 2011 Jul 21;585(14):2313-7. Epub 2011 Jun 12. PMID:21664908 doi:10.1016/j.febslet.2011.05.064

Contents


PDB ID 3asm

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OCA

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