Title

Analysis and modeling of mycolyl-transferases in the CMN group

Authors

Hemalatha Golaconda Ramulu, Swathi Adindla, Lalitha Guruprasad*

Affiliation

School of Chemistry, University of Hyderabad, Hyderabad 500 046, India

E-mail*

lgpsc@uohyd.ernet.in; * Corresponding author

Article Type

Hypothesis

Date

received May 10, 2006; revised June 14, 2006; accepted June 14, 2006; published online June 18, 2006

Abstract

Mycolyl-transferases are a family of proteins that are specifically present in the CMN (Corynebacterium, Mycobacterium and Nocardia) genera and are responsible for the synthesis of cell wall components. We modeled the three-dimensional structures of mycolyl-transfersases from Corynebacterium and Nocardia using homology modeling methods based on the crystal structures of mycolyl-transferases from M. tuberculosis. Comparison of the models revealed significant differences in their substrate binding site. Some mycolyl-transferases identified by the following Gene Ids: Nfa25110, Nfa45560, Nfa7210, Nfa38260, Nfa32420, Nfa23770, Nfa43800, Nfa30260, Dip0365, Ncgl0987, Ce1488, Ncgl0885, Ce0984, Ncgl2101, Ncgl0336, Ce0356 are associated with a relatively larger substrate binding site and amino acid residue mutations (D40N, R43D/G, S236N/A) are likely to affect binding to trehalose.

Keywords

CMN; Mycobacterium; Corynebacterium; Nocardia; mycolyl-transferases; homology modeling

Citation

Ramulu et al., Bioinformation 1(5): 161-169 (2006)

Edited by

P. Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.