A user-friendly web portal for analyzing conformational changes in structures of Mycobacterium tuberculosis

• Published in: Journal of molecular modeling 2015-10, Vol.21 (10), p.252-252, Article 252
• Main Authors: Hassan, Sameer, Thangam, Manonanthini, Vasudevan, Praveen, Kumar, G. Ramesh, Unni, Rahul, Devi, P. K. Gayathri, Hanna, Luke Elizabeth
• Format: Article
• Language: English
• Subjects: Antitubercular Agents - chemistry; Antitubercular Agents - pharmacology; Bacterial Proteins - antagonists & inhibitors; Bacterial Proteins - chemistry; Catalytic Domain; Characterization and Evaluation of Materials; Chemistry; Chemistry and Materials Science; Computational Biology - methods; Computer Appl. in Life Sciences; Computer Applications in Chemistry; Databases, Protein; Drug Discovery; Ligands; Models, Molecular; Molecular Medicine; Mycobacterium tuberculosis - chemistry; Original Paper; Protein Conformation; Protein Interaction Domains and Motifs; Quantitative Structure-Activity Relationship; Theoretical and Computational Chemistry; Web Browser
• ISSN: 1610-2940; 0948-5023
• DOI: 10.1007/s00894-015-2799-6

Initiation of the Tuberculosis Structural Consortium has resulted in the expansion of the Mycobacterium tuberculosis (MTB) protein structural database. Currently, 969 experimentally solved structures are available for 354 MTB proteins. This includes multiple crystal structures for a given protein under different functional conditions, such as the presence of different ligands or mutations. In depth analysis of the multiple structures reveal that subtle differences exist in conformations of a given protein under varied conditions. Therefore, it is immensely important to understand the conformational differences between the multiple structures of a given protein in order to select the most suitable structure for molecular docking and structure-based drug designing. Here, we introduce a web portal ( http://bmi.icmr.org.in/mtbsd/torsion.php ) that we developed to provide comparative data on the ensemble of available structures of MTB proteins, such as Cα root means square deviation (RMSD), sequence identity, presence of mutations and torsion angles. Additionally, torsion angles were used to perform principal component analysis (PCA) to identify the conformational differences between the structures. Additionally, we present a few case studies to demonstrate this database. Graphical Abstract Conformational changes seen in the structures of the enoyl-ACP reductase protein encoded by the Mycobacterial gene inhA