Structural highlights
Function
PRLA_LYSEN
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structural plasticity broadens the specificity of an engineered protease.,Bone R, Silen JL, Agard DA Nature. 1989 May 18;339(6221):191-5. PMID:2716847[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bone R, Silen JL, Agard DA. Structural plasticity broadens the specificity of an engineered protease. Nature. 1989 May 18;339(6221):191-5. PMID:2716847 doi:http://dx.doi.org/10.1038/339191a0
