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Title |
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Insights from Streptococcus pneumoniae glucose kinase structural model
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Authors |
Chaitanya Mulakayala1, Babajan Nawaz Banaganapalli1, C. M. Anuradha2, Suresh Kumar Chitta1*
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Affiliation |
1DBT-Bioinforamatics Facility (BIF) and Department of Biochemistry, 2Department of Biotechnology, Sri Krishnadevarya University College of Engineering and Technology, Sri Krishnadevaraya University, Anantapur-515 003, A.P. India
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chitta34c@gmail.com; * Corresponding authors | |
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91-8554-255644 | |
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91-8554-255644 | |
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Article Type
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Hypothesis
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Date
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received September 23, 2008; revised November 3, 2008; accepted January 8, 2009; published February 26, 2009 | |
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Abstract |
Streptococcus pneumonia is the common cause of sepsis and meningitis. Emergence of multiple antibiotic resistant strains in the community-acquired bacterium is catastrophic. Glucose kinase (GLK) is a regulatory enzyme capable of adding phosphate group to glucose in the first step of streptomycin biosynthesis. The activity of glucose kinase was regulated by the Carbon Catabolite Repression (CCR) system. Therefore, it is important to establish the structure-function relation of GLK in S. pneumoniae. However, a solved structure for S. pneumoniae GLK is not available at the protein data bank (PDB). Therefore, we created a model of GLK from S. pnemoniae using the X-ray structure of Glk from E. faecalis as template with MODELLER (a comparative modeling program). The model was validated using protein structure checking tools such as PROCHECK, WHAT IF and ProSA for reliability. The active site amino acid Asp114 in the template is retained in S. pneumoniae GLK model (Asp115). Solvent accessible surface area (ASA) analysis of the GLK model showed that known key residues playing important role in active site for ligand binding and metal ion binding are buried and hence not accessible to solvent. The information thus discussed provides insight to the molecular understanding of glucose kinase in S. pneumoniae.
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Keywords |
Glucose kinase, active site, model, homology, function | |
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Citation |
Mulakayala et al. , Bioinformation 3(7): 308-310 (2009)
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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
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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.
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