April Journal-2009.p65 - Association of Biotechnology and Pharmacy

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Current Trends in Biotechnology and Pharmacy Vol. 3 (2) 210-218, April 2009. ISSN 0973-8916 those glycine residues falling in disallowed region (Fig. 8). The overall results provided the evidences that the predicted 3-Dimensional structure of CtGH39 is acceptable and of good quality. Acknowledgments SA was supported by PhD fellowship from Indian Institute of Technology Guwahati through Ministry of Human Resource and Development, Government of India. The research work in part was supported by a project grant from Department of Biotechnology, Ministry of Science and Technology, New Delhi, India to AG. Fig. 7. Ramachandran plot analysis of CtGH39 using RAMPAGE software(24,25). It shows the various residues falling in favoured allowed and disallowed region and the Glycine residues (352 residues are in favoured region, 22 in allowed region and 10 in disallowed region) so > 90% residues have allowed conformations. 215 References 1. Johnson, E.A., Sakajoh, M., Halliwell, G., Madia, A. and Demain, A.L. (1982). Saccharification of complex cellulosic substrates by cellulase system from Clostridium thermocellum. Appl. Environ. Microbiol. 43, 1125–1132. 2. Carbohydrate active enzymes (CAZY) link (http://www.cazy.org/fam/acc_GH.html). 3. Henrissat, B. (1991). A classification of glycosyl hydrolases based on amino-acid sequence similarities. Biochem. J., 280, 309- 316. 4. Davies, G. and Henrissat, B. (1995). Structures and mechanisms of glycosyl hydrolases. Structure, 3, 853-857. 5. Henrissat, B. and Bairoch, A. (1993). New families in the classification of glycosyl hydrolases based on amino-acid sequence similarities. Biochem. J., 293, 781-788. 6. Lairson, L.L., Henrissat, B., Davies, G.J. and Withers, S.G. (2008). Glycosyltransferases: Structures, Functions and Mechanisms. Ann. Rev. Biochem., 77, 521-555. 7. Henrissat B. and Bairoch A. (1996). Updating the sequence-based classification of glycosyl hydrolases. Biochem. J., 316, 695-696. 8. Lynd, L.R, Weimer, P.J., van Zyl, W.H. and Pretorious, I.S. (2002). Microbial cellulose utilization: fundamentals and biotechnology. Microbiol. Mol. Biol. Rev., 66, 506-577. 9. Sánchez, R. and Sali, A. (2000). Comparative protein structure modeling: Introduction and practical examples with MODELLER. In: Protein Structure Prediction: Methods and Protocols. Ed: D. M. Webster. Humana Press, Totowa, NJ, 97-129. Homology modeling of family 39 glycoside hydrolase
Current Trends in Biotechnology and Pharmacy Vol. 3 (2) 210-218, April 2009. ISSN 0973-8916 217 Fig. 8. Ramachandran plot analysis of CtGH39 for general, gly, Pre-Pro, Pro using RAMPAGE (24,25). The conformations and location of each of the above is shown in individual plots having heading as general, Glycine, pre-Pro and Pro. Ahmed et al
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