2V2D
The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM
Summary for 2V2D
Entry DOI | 10.2210/pdb2v2d/pdb |
Related | 1AG1 1DKW 1IIG 1IIH 1KV5 1ML1 1MSS 1MTM 1TPD 1TPE 1TPF 1TRD 1TRI 1TSI 1TTI 1TTJ 2J24 2J27 2V0T 2V2C 3TIM 4TIM 5TIM 6TIM |
Descriptor | TRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL, PHOSPHATE ION (3 entities in total) |
Functional Keywords | gluconeogenesis, lipid synthesis, engineering, pentose shunt, point mutation, tim, a178l, loop6, hinge, loop-6, enzyme, isomerase, fatty acid biosynthesis, triosephosphate isomerase, glycosome, monomeric, tim-barrel, glycolysis |
Biological source | TRYPANOSOMA BRUCEI BRUCEI |
Total number of polymer chains | 1 |
Total formula weight | 26170.80 |
Authors | Alahuhta, M.,Casteleijn, M.G.,Neubauer, P.,Wierenga, R.K. (deposition date: 2007-06-05, release date: 2008-02-19, Last modification date: 2023-12-13) |
Primary citation | Alahuhta, M.,Casteleijn, M.G.,Neubauer, P.,Wierenga, R.K. Structural Studies Show that the A178L Mutation in the C-Terminal Hinge of the Catalytic Loop-6 of Triosephosphate Isomerase (Tim) Induces a Closed- Like Conformation in Dimeric and Monomeric Tim. Acta Crystallogr.,Sect.D, 64:178-, 2008 Cited by PubMed: 18219118DOI: 10.1107/S0907444907059021 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
Download full validation report