Robustness and evolvability in the functional anatomy of a PER-ARNT-SIM (PAS) domain.

ABSTRACT: The robustness of proteins against point mutations implies that only a small subset of residues determines functional properties. We test this prediction using photoactive yellow protein (PYP), a 125-residue prototype of the PER-ARNT-SIM (PAS) domain superfamily of signaling proteins. PAS domains are defined by a small number of conserved residues of unknown function. We report high-throughput biophysical measurements on a complete Ala scan set of purified PYP mutants. The dataset of 1,193 values on active site properties, functional kinetics, stability, and production level reveals that 124 mutants retain the characteristic photocycle of PYP, but that the majority of substitutions significantly alter functional properties. Only 35% of substitutions that strongly affect function are locate

SUBMITTER: Philip AF 

PROVIDER: S-EPMC2964196 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature