Yersinia
pestis, the causative organism of Plague, is widely recognized as a potential
bioterrorism threat. Due to the absence of homologs in human, Shikimate Kinase
(SK) is considered as an excellent drug target in several bacterial and
protozoan parasites.
Ample literature evidences confirm the suitability of this
protein as a good target. Therefore, Shikimate Kinase of Shikimate pathway inYersinia pestis represents an attractive drug target. In the present study, a
clustering approach was undertaken to select the proper representative for
Shikimate Kinase sequences belonging to Yersinia pestis for structure
determination.
Three-dimensional models of the enzyme for KFB61218.1 (SK1),
EFA47400.1 (SK2) and WP_016255950.1 (SK3) were generated using a comparative
molecular modeling approach where structures were developed using the single
specific template as well as multiple closely associated templates. Thestructures of Shikimate Kinase developed using comparative modeling were evaluatedfor stereochemical quality using various structural validation tools. Results
from structural assessment tools indicated the reasonably good quality of
models.
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