An NMR and MD study of complexes of bacteriophage lambda lysozyme with tetra- and hexa-N-acetylchitohexaose.
Bacteriophage lambda
/ chemistry
Catalytic Domain
/ drug effects
Enzyme Inhibitors
/ chemistry
Molecular Docking Simulation
Molecular Dynamics Simulation
Muramidase
/ antagonists & inhibitors
Nuclear Magnetic Resonance, Biomolecular
Oligosaccharides
/ chemistry
Protein Binding
Protein Conformation
/ drug effects
NMR spectroscopy
ligand binding
lysozymes
molecular dynamics
oligosaccharides
Journal
Proteins
ISSN: 1097-0134
Titre abrégé: Proteins
Pays: United States
ID NLM: 8700181
Informations de publication
Date de publication:
01 2020
01 2020
Historique:
received:
24
05
2019
revised:
02
07
2019
accepted:
06
07
2019
pubmed:
12
7
2019
medline:
21
11
2020
entrez:
12
7
2019
Statut:
ppublish
Résumé
The X-ray structure of lysozyme from bacteriophage lambda (λ lysozyme) in complex with the inhibitor hexa-N-acetylchitohexaose (NAG6) (PDB: 3D3D) has been reported previously showing sugar units from two molecules of NAG6 bound in the active site. One NAG6 is bound with four sugar units in the ABCD sites and the other with two sugar units in the E'F' sites potentially representing the cleavage reaction products; each NAG6 cross links two neighboring λ lysozyme molecules. Here we use NMR and MD simulations to study the interaction of λ lysozyme with the inhibitors NAG4 and NAG6 in solution. This allows us to study the interactions within the complex prior to cleavage of the polysaccharide.
Identifiants
pubmed: 31294851
doi: 10.1002/prot.25770
pmc: PMC6916166
doi:
Substances chimiques
Enzyme Inhibitors
0
Oligosaccharides
0
N-acetylchitohexaose
38854-46-5
Muramidase
EC 3.2.1.17
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
82-93Subventions
Organisme : Austrian Science Fund FWF
ID : W 1224
Pays : Austria
Organisme : Austrian Science Fund FWF
ID : BioToP grant number W1224
Pays : Austria
Organisme : Wellcome Trust
ID : Grant No. 079440
Pays : United Kingdom
Informations de copyright
© 2019 The Authors. Proteins: Structure, Function, and Bioinformatics published by Wiley Periodicals, Inc.
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