Crystal Structure of Triosephosphate Isomerase Complexed with 2-Phosphoglycolate at 0.83-Å Resolution

摘要: Abstract The atomic resolution structure ofLeishmania mexicana triosephosphate isomerase complexed with 2-phosphoglycolate shows that this transition state analogue is bound in two conformations. Also for the side chain of catalytic glutamate, Glu167, conformations are observed. In both conformations, a very short hydrogen bond exists between carboxylate group ligand and glutamate. distance O11 PGA Oe2 Glu167 2.61 2.55 A major minor respectively. either conformation, Oe1 hydrogen-bonded to water network connecting bulk solvent. This also occurs mutually exclusive arrangements. Despite structural disorder active site, C termini β strands construct site display least anisotropy compared rest protein. loops following these various degrees anisotropy, tip dimer interface loop 3 having low C-terminal region 6 highest anisotropy. pyrrolidine ring Pro168 at N-terminal strained planar conformation facilitate opening product release.