What can structure tell us about in vivo function? The case of aminoglycoside-resistance genes

M. Vetting; S. L. Roderick; S. Hegde; S. Magnet; J. S. Blanchard

doi:10.1042/BST0310520

What can structure tell us about in vivo function? The case of aminoglycoside-resistance genes

M. Vetting, S. L. Roderick, S. Hegde, S. Magnet, J. S. Blanchard

Biochemistry

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

Resistance to antibiotics used in the treatment of bacterial infections is an expanding clinical problem. Aminoglycosides, one of the oldest classes of natural product antibiotics, exert their bactericidal effect as the result of inhibiting bacterial protein synthesis by binding to the acceptor site of the 30 S ribosomal subunit. The most common mechanism of clinical resistance to aminoglycosides results from the expression of enzymes that covalently modify the aminoglycoside. We will discuss the enzymology and structure of two representative chromosomally encoded aminoglycoside N-acetyltransferases, Mycabacterium tuberculasis AAC(2′)-lc and Salmanella enterica AAC(6′)-ly, and speculate about their possible physiological function and substrates.

Original language	English (US)
Pages (from-to)	520-522
Number of pages	3
Journal	Biochemical Society transactions
Volume	31
Issue number	3
DOIs	https://doi.org/10.1042/BST0310520
State	Published - Jun 1 2003

Keywords

Acetyltransferase
Aminoglycoside
Antibiotic resistance
Mycobacterium tuberculosis
Salmonella enterica

ASJC Scopus subject areas

Biochemistry

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1042/BST0310520

Cite this

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abstract = "Resistance to antibiotics used in the treatment of bacterial infections is an expanding clinical problem. Aminoglycosides, one of the oldest classes of natural product antibiotics, exert their bactericidal effect as the result of inhibiting bacterial protein synthesis by binding to the acceptor site of the 30 S ribosomal subunit. The most common mechanism of clinical resistance to aminoglycosides results from the expression of enzymes that covalently modify the aminoglycoside. We will discuss the enzymology and structure of two representative chromosomally encoded aminoglycoside N-acetyltransferases, Mycabacterium tuberculasis AAC(2′)-lc and Salmanella enterica AAC(6′)-ly, and speculate about their possible physiological function and substrates.",

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AU - Vetting, M.

AU - Roderick, S. L.

AU - Hegde, S.

AU - Magnet, S.

AU - Blanchard, J. S.

PY - 2003/6/1

Y1 - 2003/6/1

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AB - Resistance to antibiotics used in the treatment of bacterial infections is an expanding clinical problem. Aminoglycosides, one of the oldest classes of natural product antibiotics, exert their bactericidal effect as the result of inhibiting bacterial protein synthesis by binding to the acceptor site of the 30 S ribosomal subunit. The most common mechanism of clinical resistance to aminoglycosides results from the expression of enzymes that covalently modify the aminoglycoside. We will discuss the enzymology and structure of two representative chromosomally encoded aminoglycoside N-acetyltransferases, Mycabacterium tuberculasis AAC(2′)-lc and Salmanella enterica AAC(6′)-ly, and speculate about their possible physiological function and substrates.

KW - Acetyltransferase

KW - Aminoglycoside

KW - Antibiotic resistance

KW - Mycobacterium tuberculosis

KW - Salmonella enterica

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What can structure tell us about in vivo function? The case of aminoglycoside-resistance genes

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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