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Title |
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Structural and functional characterization of HMG-COA reductase from Artemisia annua |
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Authors |
Usha Kiran1, Mauji Ram2, Mather Ali Khan2, Salim Khan5, Prabhakar Jha3, Afshar Alam4, Malik Zainul Abdin2* |
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Affiliation |
1Faculty of Interdisciplinary Research Studies, Jamia Hamdard, New Delhi-110062, India. 2Department of Biotechnology, Faculty of Science, Jamia Hamdard, New Delhi-110062, India. 3Department of Botany, Faculty of Science, Jamia Hamdard, New Delhi-110062, India.4Department of Computer Science, Jamia Hamdard, New Delhi-110062, India. 5Department of Botany and Microbiology, College of Science, King Saud University, Riyadh 11451, Kingdom of Saudi Arabia. |
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mzabdin@rediffmail.com *Corresponding Author |
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Phone |
+91-11-26059688; Extn: 5583 |
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Article Type |
Hypothesis |
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Date |
Received June 16, 2010; Accepted August 20, 2010; Published September 20, 2010 |
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Abstract |
Plants synthesize a great variety of isoprenoid products that are required not only for normal growth and development but also for their adaptive responses to environmental challenges. However, despite the remarkable diversity in the structure and function of plant isoprenoids, they all originate from a single metabolic precursor, mevalonic acid. The synthesis of mevalonic acid is catalysed by the enzyme, 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMG- CoA reductase). The analysis of the amino acid sequence of HMG-CoA reductase from Artemisia annua L. plant showed that it belongs to class I HMG-CoA reductase family. The three dimensional structure of HMG-CoA reductase of Artemisia annua has been generated from amino acid sequence using homology modelling with backbone structure of human HMG-CoA reductase as template. The model was generated using the SWISS MODEL SERVER. The generated 3-D structure of HMG-CoA reductase was evaluated at various web interfaced servers to checks the stereo interfaced quality of the structure in terms of bonds, bond angles, dihedral angles and non-bonded atom-atom distances, structural as well as functional domains etc. The generated model was visualized using the RASMOL. Structural analysis of HMG-CoA reductase from Artemisia annua L. plant hypothesize that the N and C-terminals are positioned in cytosol by the two membrane spanning helices and the C-terminals domain shows similarity to the human HMG-CoA reductase enzyme indicating that they both had potential catalytic similarities.
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Keywords
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Mevalonic acid, Hydroxy-3-methylglutaryl coenzyme A, Artemisia annua and RASMOL. |
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Citation |
Abdin et al. Bioinformation 5(4): 146-149 (2010) |
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Edited by |
P. Kangueane
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ISSN |
0973-2063
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Publisher |
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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. |