NAD+ specificity of bacterial DNA ligase revealed Journal Article


Author: Shuman, S.
Article Title: NAD+ specificity of bacterial DNA ligase revealed
Abstract: In this issue of Structure, crystallographic snapshots of a bacterial DNA ligase in complexes with its substrate NAD+ and its product NMN are revealed (Gajiwala and Pinko, 2004). The structures illustrate a novel reaction of DNA ligase and highlight the NMN binding site as a target for new antimicrobials.
Keywords: nonhuman; gene targeting; bacteria (microorganisms); antiinfective agent; amino terminal sequence; escherichia coli; short survey; binding site; crystal structure; protein structure, tertiary; molecular structure; catalysis; conformation; dna binding; polydeoxyribonucleotide synthase; enzyme specificity; enzyme substrate complex; bacterial dna; dna, bacterial; nad; chemical reaction; enzyme synthesis; nicotinamide adenine dinucleotide; dna ligases; adenylation; crystallography; bacteria; priority journal; nicotinamide nucleotide; nicotinamide mononucleotide
Journal Title: Structure
Volume: 12
Issue: 8
ISSN: 0969-2126
Publisher: Cell Press  
Date Published: 2004-08-01
Start Page: 1335
End Page: 1336
Language: English
DOI: 10.1016/j.str.2004.07.002
PUBMED: 15296724
PROVIDER: scopus
DOI/URL:
Notes: Cited By (since 1996):3 -- Export Date: 16 June 2014 -- CODEN: STRUE -- Source: Scopus
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  1. Stewart H Shuman
    546 Shuman