Published in

Elsevier, Biophysical Journal, 9(98), p. L38-L40, 2010

DOI: 10.1016/j.bpj.2010.01.006

Links

Tools

Export citation

Search in Google Scholar

Tryptophan as a Molecular Shovel in the Glycosyl Transfer Activity of Trypanosoma cruzi Trans-sialidase

Journal article published in 2010 by Felicity L. Mitchell, Steven M. Miles, João Neres ORCID, Elena V. Bichenkova, Richard A. Bryce, S. M. Miles J Neres E V. Bichenkova R A. Bryce F. L. Mitchell
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

Full text: Download

Green circle
Preprint: archiving allowed
Upload
Orange circle
Postprint: archiving restricted
Upload
Red circle
Published version: archiving forbidden
Policy details
Data provided by SHERPA/RoMEO

Abstract

Molecular dynamics investigations into active site plasticity of Trypanosoma cruzi trans-sialidase, a protein implicated in Chagas disease, suggest that movement of the Trp(312) loop plays an important role in the enzyme's sialic acid transfer mechanism. The observed Trp(312) flexibility equates to a molecular shovel action, which leads to the expulsion of the donor aglycone leaving group from the catalytic site. These computational simulations provide detailed structural insights into sialyl transfer by the trans-sialidase and may aid the design of inhibitors effective against this neglected tropical disease.