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'''STRUCTURE OF THE ADENYLATION DOMAIN OF AN NAD+ DEPENDENT LIGASE''' | '''STRUCTURE OF THE ADENYLATION DOMAIN OF AN NAD+ DEPENDENT LIGASE''' | ||
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==Reference== | ==Reference== | ||
Structure of the adenylation domain of an NAD+-dependent DNA ligase., Singleton MR, Hakansson K, Timson DJ, Wigley DB, Structure. 1999 Jan 15;7(1):35-42. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10368271 10368271] | Structure of the adenylation domain of an NAD+-dependent DNA ligase., Singleton MR, Hakansson K, Timson DJ, Wigley DB, Structure. 1999 Jan 15;7(1):35-42. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10368271 10368271] | ||
[[Category: Geobacillus stearothermophilus]] | [[Category: Geobacillus stearothermophilus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Timson, D J.]] | [[Category: Timson, D J.]] | ||
[[Category: Wigley, D B.]] | [[Category: Wigley, D B.]] | ||
[[Category: | [[Category: Dna replication]] | ||
[[Category: | [[Category: Ligase]] | ||
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Revision as of 07:54, 2 May 2008
STRUCTURE OF THE ADENYLATION DOMAIN OF AN NAD+ DEPENDENT LIGASE
Overview
BACKGROUND: DNA ligases catalyse phosphodiester bond formation between adjacent bases in nicked DNA, thereby sealing the nick. A key step in the catalytic mechanism is the formation of an adenylated DNA intermediate. The adenyl group is derived from either ATP (in eucaryotes and archaea) or NAD+4 (in bacteria). This difference in cofactor specificity suggests that DNA ligase may be a useful antibiotic target. RESULTS: The crystal structure of the adenylation domain of the NAD+-dependent DNA ligase from Bacillus stearothermophilus has been determined at 2.8 A resolution. Despite a complete lack of detectable sequence similarity, the fold of the central core of this domain shares homology with the equivalent region of ATP-dependent DNA ligases, providing strong evidence for the location of the NAD+-binding site. CONCLUSIONS: Comparison of the structure of the NAD+4-dependent DNA ligase with that of ATP-dependent ligases and mRNA-capping enzymes demonstrates the manifold utilisation of a conserved nucleotidyltransferase domain within this family of enzymes. Whilst this conserved core domain retains a common mode of nucleotide binding and activation, it is the additional domains at the N terminus and/or the C terminus that provide the alternative specificities and functionalities in the different members of this enzyme superfamily.
About this Structure
1B04 is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
Reference
Structure of the adenylation domain of an NAD+-dependent DNA ligase., Singleton MR, Hakansson K, Timson DJ, Wigley DB, Structure. 1999 Jan 15;7(1):35-42. PMID:10368271 Page seeded by OCA on Fri May 2 10:54:17 2008
