Allosteric transition and binding of small molecule effectors causes curvature change in central β-sheets of selected enzymes.

ABSTRACT: A quantitative description of allosteric transition remains a significant science challenge. Many allosteric enzymes contain a central β-sheet in their catalytic domain. When an allosteric protein undergoes the transition between T (tense) and R (relaxed) allosteric states, this central β-sheet undergoes a conformational change. A traditional method of measuring this change, the root mean square deviation (RMSD), appears to be inadequate to describe such changes in meaningful quantitative manner. We designed a novel quantitative method to demonstrate this conformational transition by measuring the change in curvature of the central β-sheet when enzymes transition between allosteric states. The curvature was established by calculating the semiaxes of a 3-D hyperboloid fitted by least square

SUBMITTER: Tolonen E 

PROVIDER: S-EPMC4127431 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature