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
.