Structure of the adenylation domain of an NAD<sup>+</sup>-dependent DNA ligase
Data(s) |
15/01/1999
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Resumo |
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.<br/><br/>Results: The crystal structure of the adenylation domain of the NAD+-dependent DNA ligase from Bacillus stearothermophilus has been determined at 2.8 Å 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.<br/><br/>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. |
Identificador |
http://dx.doi.org/10.1016/S0969-2126(99)80007-0 http://www.scopus.com/inward/record.url?scp=0033555464&partnerID=8YFLogxK |
Idioma(s) |
eng |
Direitos |
info:eu-repo/semantics/restrictedAccess |
Fonte |
Singleton , M R , Håkansson , K , Timson , D & Wigley , D B 1999 , ' Structure of the adenylation domain of an NAD + -dependent DNA ligase ' Structure , vol 7 , no. 1 , pp. 35-42 . DOI: 10.1016/S0969-2126(99)80007-0 |
Palavras-Chave | #/dk/atira/pure/subjectarea/asjc/1300/1312 #Molecular Biology #/dk/atira/pure/subjectarea/asjc/1300/1315 #Structural Biology |
Tipo |
article |