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. 2015;16 Suppl 2(Suppl 2):S14.
doi: 10.1186/1471-2164-16-S2-S14. Epub 2015 Jan 21.

Mechanistic analysis elucidating the relationship between Lys96 mutation in Mycobacterium tuberculosis pyrazinamidase enzyme and pyrazinamide susceptibility

Chakshu Vats, Jaspreet Dhanjal, Sukriti Goyal, Ankita Gupta, Navneeta Bharadvaja, Abhinav Grover

Mechanistic analysis elucidating the relationship between Lys96 mutation in Mycobacterium tuberculosis pyrazinamidase enzyme and pyrazinamide susceptibility

Chakshu Vats et al. BMC Genomics. 2015.
No abstract available

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Figures

Figure 1
Figure 1
Ribbon representation of the superimposition of structures of the native and mutant M. tuberculosis PncA protein.
Figure 2
Figure 2
Depiction of hydrogen bond interactions in A) native protein bound to PZA after docking, B) native protein bound with PZA after MD simulations, C) docked mutant PncA-PZA complex, D) mutant protein bound to PZA post MD simulations.
Figure 3
Figure 3
Hydrophobic interaction pattern in A) native protein bound to PZA after docking, B) native protein bound with PZA after MD simulations, C) docked mutant PncA-PZA complex, D) mutant protein bound to PZA post MD simulations.
Figure 4
Figure 4
Graph showing the RMSD of backbone of native unbound protein, native bound to PZA, mutant protein in unbound form and mutant protein in complex with PZA.
Figure 5
Figure 5
Radius of gyration of native and mutant protein in complex with PZA.
Figure 6
Figure 6
Root mean square fluctuation of all the residues in native protein bound to PZA, mutant protein in unbound form and mutant protein in complex with PZA.
See this image and copyright information in PMC

References

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