Structural plasticity broadens the specificity of an engineered protease

Nature. 1989 May 18;339(6221):191-5. doi: 10.1038/339191a0.

Abstract

The substrate specificity of alpha-lytic protease has been changed dramatically, with a concomitant increase in activity, by replacing an active-site Met with Ala. The substrate specificity of both this mutant and another similar mutant are extraordinarily broad. X-ray crystallographic analysis shows that structural plasticity, a combination of alternate side-chain conformations and binding-site flexibility, allows both large and small substrates to be well accommodated.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Crystallography
  • Molecular Structure*
  • Mutation
  • Protein Conformation
  • Serine Endopeptidases* / genetics
  • Substrate Specificity*

Substances

  • Serine Endopeptidases
  • myxobacter alpha-lytic proteinase