Proposal for new catalytic roles for two invariant residues in Escherichia coli ribonuclease HI.

doi:10.1093/protein/9.10.857

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Article

Proposal for new catalytic roles for two invariant residues in Escherichia coli ribonuclease HI.

Protein engineering - 1 Oct 1996

Kashiwagi T, Jeanteur D, Haruki M, Katayanagi K, Kanaya S, Morikawa K

Abstract excerpt

Three mutants of Escherichia coli ribonuclease HI, in which an invariant acidic residue Asp134 was replaced, were crystallized, and their three-dimensional structures were determined by X-ray crystallography. The D134A mutant is completely inactive, whereas the other two mutants, D134H and D134N,...

Topics

Aspartic Acid
Binding Sites
Crystallization
Crystallography, X-Ray
Electrons
Escherichia coli
Hydrogen-Ion Concentration
Mutation
Protein Binding
Protein Structure, Secondary
Ribonuclease H

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