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Volume 98, Issue 9, Pages L38-L40 (May 2010)

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1 Volume 98, Issue 9, Pages L38-L40 (May 2010)
Tryptophan as a Molecular Shovel in the Glycosyl Transfer Activity of Trypanosoma cruzi Trans-sialidase  Felicity L. Mitchell, Steven M. Miles, João Neres, Elena V. Bichenkova, Richard A. Bryce  Biophysical Journal  Volume 98, Issue 9, Pages L38-L40 (May 2010) DOI: /j.bpj Copyright © 2010 Biophysical Society Terms and Conditions

2 Scheme 1 First step of sialyl transfer catalyzed by TcTS.
Biophysical Journal  , L38-L40DOI: ( /j.bpj ) Copyright © 2010 Biophysical Society Terms and Conditions

3 Figure 1 Flexibility of the Tyr119 and Trp312 residues of TcTS during the molecular dynamics simulation of the sialyl enzyme covalent intermediate complexed with lactose: Tyr119 switches from the stacked to a rotated position and Trp312 moves between stacked and open conformations. Biophysical Journal  , L38-L40DOI: ( /j.bpj ) Copyright © 2010 Biophysical Society Terms and Conditions

4 Figure 2 Selected steps from along the MD trajectory of the sialylated-enzyme/lactose complex, III. (a) Initially Tyr119 is in the stacking position and the Trp312 loop is stacked (b) At 22 ns, the Tyr119 rotates away from the stack, followed by a Trp312 motion to shift the Trp312/lactose portion of the stack (c) Full opening of the Trp312 loop enables lactose to vacate the active site by 32 ns. Biophysical Journal  , L38-L40DOI: ( /j.bpj ) Copyright © 2010 Biophysical Society Terms and Conditions

5 Figure 3 Dynamics of sialylated TcTS/lactose (III): time series of (a) side-chain dihedral angle, χ1, of Tyr119; (b) intercentroid distance between Tyr119 and Trp312 rings; and (c) distance between centers of mass of sialic acid and lactose. Biophysical Journal  , L38-L40DOI: ( /j.bpj ) Copyright © 2010 Biophysical Society Terms and Conditions


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