Next Article in Journal
Identification of the NADP+ Structural Binding Site and Coenzyme Effect on the Fused G6PD::6PGL Protein from Giardia lamblia
Previous Article in Journal
Mercury and Alzheimer’s Disease: Hg(II) Ions Display Specific Binding to the Amyloid-β Peptide and Hinder Its Fibrillization
Open AccessArticle

Comparative Structural Analysis of Different Mycobacteriophage-Derived Mycolylarabinogalactan Esterases (Lysin B)

1
Department of Microbiology and Immunology, Faculty of Pharmacy, Nahda University, Beni-Suef 62513, Egypt
2
Biotechnology, Department of Chemistry, Center for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden
3
Department of Microbiology and Immunology, Faculty of Pharmacy, Al-Azhar University, Assiut 71524, Egypt
4
Department of Microbiology and Immunology, Faculty of Pharmacy, Beni-Suef University, Beni-Suef 26511, Egypt
5
Department of Microbiology and Immunology, Faculty of Pharmacy, Cairo University, Cairo 11562, Egypt
*
Author to whom correspondence should be addressed.
Biomolecules 2020, 10(1), 45; https://doi.org/10.3390/biom10010045
Received: 6 October 2019 / Revised: 2 December 2019 / Accepted: 25 December 2019 / Published: 27 December 2019
(This article belongs to the Section Bioinformatics and Systems Biology)
Mycobacteriophage endolysins have emerged as a potential alternative to the current antimycobacterial agents. This study focuses on mycolylarabinogalactan hydrolase (LysB) enzymes of the α/β-hydrolase family, which disrupt the unique mycolic acid layer of mycobacterium cell wall. Multiple sequence alignment and structural analysis studies showed LysB-D29, the only enzyme with a solved three-dimensional structure, to share several common features with esterases (lacking lid domain) and lipases (acting on long chain lipids). Sequence and structural comparisons of 30 LysB homology models showed great variation in domain organizations and total protein length with major differences in the loop-5 motif harboring the catalytic histidine residue. Docking of different p-nitrophenyl ligands (C4-C18) to LysB-3D models revealed that the differences in length and residues of loop-5 contributed towards wide diversity of active site conformations (long tunnels, deep and superficial funnels, shallow bowls, and a narrow buried cave) resembling that of lipases, cutinases, and esterases. A set of seven LysB enzymes were recombinantly produced; their activity against p-nitrophenyl esters could be related to their active site conformation and acyl binding site. LysB-D29 (long tunnel) showed the highest activity with long chain p-nitrophenyl palmitate followed by LysB-Omega (shallow bowl) and LysB-Saal (deep funnel). View Full-Text
Keywords: mycolylarabinogalactan esterases; α/β-hydrolase family; LysB homology models; multiple sequence alignment; molecular docking mycolylarabinogalactan esterases; α/β-hydrolase family; LysB homology models; multiple sequence alignment; molecular docking
Show Figures

Figure 1

MDPI and ACS Style

Korany, A.H.; Abouhmad, A.; Bakeer, W.; Essam, T.; Amin, M.A.; Hatti-Kaul, R.; Dishisha, T. Comparative Structural Analysis of Different Mycobacteriophage-Derived Mycolylarabinogalactan Esterases (Lysin B). Biomolecules 2020, 10, 45.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop