The critical role of the loops of triosephosphate isomerase for its oligomerization, dynamics, and functionality.

ABSTRACT: Triosephosphate isomerase (TIM) catalyzes the reaction to convert dihydroxyacetone phosphate into glyceraldehyde 3-phosphate, and vice versa. In most organisms, its functional oligomeric state is a homodimer; however, tetramer formation in hyperthermophiles is required for functional activity. The tetrameric TIM structure also provides added stability to the structure, enabling it to function at more extreme temperatures. We apply Principal Component Analysis to find that the TIM structure space is clearly divided into two groups--the open and the closed TIM structures. The distribution of the structures in the open set is much sparser than that in the closed set, showing a greater conformational diversity of the open structures. We also apply the Elastic Network Model to four different TI

SUBMITTER: Katebi AR 

PROVIDER: S-EPMC3926746 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature