Abstract
Natural(ly) fit: The X-ray crystal structure of the bacterial membrane protein MraY in complex with its natural product inhibitor muraymycin D2 is discussed. MraY catalyzes one of the membrane-associated steps in peptidoglycan biosynthesis and, therefore, represents a promising target for novel antibiotics. Structural insights derived from the protein-inhibitor complex might now pave the way for the development of new antimicrobial drugs.
Keywords:
antibiotics; medicinal chemistry; natural products; peptidoglycans; protein crystallography.
© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
MeSH terms
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Anti-Bacterial Agents / chemistry
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Anti-Bacterial Agents / pharmacology*
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Bacteria / chemistry
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Bacteria / drug effects
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Bacteria / enzymology*
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Bacteria / metabolism
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Bacterial Infections / drug therapy
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Bacterial Infections / microbiology
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Bacterial Proteins / antagonists & inhibitors*
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism
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Biological Products / chemistry
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Biological Products / pharmacology*
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Crystallography, X-Ray
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Humans
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Molecular Docking Simulation
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Nucleosides / chemistry
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Nucleosides / pharmacology*
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Peptides / chemistry
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Peptides / pharmacology*
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Peptidoglycan / metabolism
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Transferases (Other Substituted Phosphate Groups)
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Transferases / antagonists & inhibitors*
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Transferases / chemistry
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Transferases / metabolism
Substances
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Anti-Bacterial Agents
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Bacterial Proteins
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Biological Products
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Nucleosides
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Peptides
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Peptidoglycan
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muraymycin D2
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Transferases
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Transferases (Other Substituted Phosphate Groups)
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mraY protein, Bacteria