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Structures and mechanisms of the mycothiol biosynthetic enzymes.

ABSTRACT: In the past decade, the genes encoding all four enzymes responsible for the biosynthesis of mycothiol in Mycobacterium tuberculosis have been identified. Orthologs of each of these have been stably expressed and structurally characterized. The chemical mechanisms of all the four have also been studied. Because of the unique phylogenetic distribution of mycothiol, and the enzymes responsible for its biosynthesis, these enzymes represent interesting potential targets for antimycobacterial agents.

SUBMITTER: Fan F

PROVIDER: S-EPMC2749902 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature

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Structures and mechanisms of the mycothiol biosynthetic enzymes.

Fan Fan F Vetting Matthew W MW Frantom Patrick A PA Blanchard John S JS

Current opinion in chemical biology 20090819 4

In the past decade, the genes encoding all four enzymes responsible for the biosynthesis of mycothiol in Mycobacterium tuberculosis have been identified. Orthologs of each of these have been stably expressed and structurally characterized. The chemical mechanisms of all the four have also been studied. Because of the unique phylogenetic distribution of mycothiol, and the enzymes responsible for its biosynthesis, these enzymes represent interesting potential targets for antimycobacterial agents. ...[more]

PMID: 19699138

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Project description:The SARS coronavirus (SARS-CoV) replicase gene encodes 16 nonstructural proteins (nsps) with multiple enzymatic activities. Several of these enzymes are common components of replication complexes of other plus-strand RNA viruses, such as picornavirus 3C-like protease, papain-like protease, RNA-dependent RNA polymerase, RNA helicase, and ribose 2′-O-methyltransferase activities, while others such as exoribonuclease, endoribonuclease, and adenosine diphosphate-ribose 1″-phosphatase activities, are rarely or not conserved in viruses outside the order Nidovirales. The latter enzymes are believed to be involved in unique metabolic pathways used by coronaviruses to (1) replicate and transcribe their extremely large RNA genomes, and (2) interfere with cellular functions and antiviral host responses. Since the global outbreak of SARS in 2003, major efforts have been made to elucidate the structures of the protein components of the SARS-CoV replication/transcription complex. Thus, in less than 5 years, the structures of as many as 16 SARS-CoV proteins or functional domains have been determined. Remarkably, eight of these 16 structures had novel folds, illustrating the uniqueness of the coronavirus replicative machinery. Furthermore, several new protein functions and potential drug targets have been identified in these studies. Current structural studies mainly focus on the few remaining proteins for which no structural information is available and larger protein complexes comprised of different nsps. The studies aim at obtaining detailed information on the functions and macromolecular assembly of the coronavirus replication/transcription machinery which, over a long period of time, may be used to develop selective antiviral drugs. This chapter reviews structural information on the SARS-CoV macro domain (ADRP) as well as nsps 7, 8, 9, and 15 and summarizes our current knowledge of active-site residues and intermolecular interactions of these proteins.

Dataset Information

Structures and mechanisms of the mycothiol biosynthetic enzymes.

Publications

Structures and mechanisms of the mycothiol biosynthetic enzymes.

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