1tph
1.8 ANGSTROMS CRYSTAL STRUCTURE OF WILD TYPE CHICKEN TRIOSEPHOSPHATE ISOMERASE-PHOSPHOGLYCOLOHYDROXAMATE COMPLEX
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OverviewOverview
The crystal structure of recombinant chicken triosephosphate isomerase, (TIM, E.C. 5.3.1.1) complexed with the intermediate analogue, phosphoglycolohydroxamate (PGH) has been solved by the method of molecular, replacement and refined to an R-factor of 18.5% at 1.8-A resolution. The, structure is essentially identical to that of the yeast TIM-PGH complex, [Davenport, R. C., et al. (1991) Biochemistry 30, 5821-5826] determined, earlier and refined at comparable resolution. This identity extends to the, high-energy conformations of the active-site residues Lys13 and Ser211, as, well as the positions of several bound water molecules that are retained, in the active site when PGH is bound. Comparison with the structure of, uncomplexed chicken TIM shows that the catalytic base, Glu165, moves, several angstroms when PGH binds. This movement may provide a trigger for, a larger conformational change, one of 7 A, in a loop near the active, site, which folds down like a lid to shield the bound inhibitor and, catalytic residues from contact with bulk solvent. These same, conformational changes were seen in crystalline yeast TIM upon binding of, PGH; their occurrence here in a different crystal form of TIM eliminates, the possibility that they are an artifact of crystal packing.
About this StructureAbout this Structure
1TPH is a Single protein structure of sequence from Gallus gallus with PGH as ligand. Active as Triose-phosphate isomerase, with EC number 5.3.1.1 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution., Zhang Z, Sugio S, Komives EA, Liu KD, Knowles JR, Petsko GA, Ringe D, Biochemistry. 1994 Mar 15;33(10):2830-7. PMID:8130195
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