1MSS

Three new crystal structures of point mutation variants of monoTIM: conformational flexibility of loop-1, loop-4 and loop-8.

(1995) Structure 3: 669-679

• PubMed: 8591044 Search on PubMed
• DOI: https://doi.org/10.1016/s0969-2126(01)00202-7
• Primary Citation of Related Structures:  
  1MSS, 1TTI, 1TTJ


• PubMed Abstract: 
  

  Wild-type triosephosphate isomerase (TIM) is a very stable dimeric enzyme. This dimer can be converted into a stable monomeric protein (monoTIM) by replacing the 15-residue interface loop (loop-3) by a shorter, 8-residue, loop. The crystal structure of monoTIM shows that two active-site loops (loop-1 and loop-4), which are at the dimer interface in wild-type TIM, have acquired rather different structural properties. Nevertheless, monoTIM has residual catalytic activity.

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Organizational Affiliation: 

EMBL, Heidelberg, Germany.