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

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ID: 74735
2019
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Abstract
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 -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 -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 -nitrophenyl palmitate followed by LysB-Omega (shallow bowl) and LysB-Saal (deep funnel).
Reference Key
korany2019comparativebiomolecules Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Korany, Ahmed H;Abouhmad, Adel;Bakeer, Walid;Essam, Tamer;Amin, Magdy A;Hatti-Kaul, Rajni;Dishisha, Tarek;
Journal Biomolecules
Year 2019
DOI
E45
URL
Keywords
molecular docking lysb homology models multiple sequence alignment mycolylarabinogalactan esterases α/β-hydrolase family

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