Comparative Structural Analysis of Different Mycobacteriophage-Derived Mycolylarabinogalactan Esterases (Lysin B).
LysB homology models
molecular docking
multiple sequence alignment
mycolylarabinogalactan esterases
α/β-hydrolase family
Journal
Biomolecules
ISSN: 2218-273X
Titre abrégé: Biomolecules
Pays: Switzerland
ID NLM: 101596414
Informations de publication
Date de publication:
27 12 2019
27 12 2019
Historique:
received:
06
10
2019
revised:
02
12
2019
accepted:
25
12
2019
entrez:
2
1
2020
pubmed:
2
1
2020
medline:
23
9
2020
Statut:
epublish
Résumé
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
Identifiants
pubmed: 31892223
pii: biom10010045
doi: 10.3390/biom10010045
pmc: PMC7022511
pii:
doi:
Substances chimiques
Galactans
0
mycolylarabinogalactan
0
Esterases
EC 3.1.-
Types de publication
Comparative Study
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
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