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: 18219118 DOI: 10.1107/S0907444907059021 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.3 Å)

Structure validation