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1TAE

Structural rearrangement accompanying NAD+ synthesis within a bacterial DNA ligase crystal

Summary for 1TAE
Entry DOI10.2210/pdb1tae/pdb
Related1TA8
DescriptorDNA ligase, NAD-dependent, SULFATE ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 entities in total)
Functional Keywordsnucleotidyl transferase fold, ligase
Biological sourceEnterococcus faecalis
Total number of polymer chains4
Total formula weight157135.94
Authors
Gajiwala, K.S.,Pinko, C. (deposition date: 2004-05-19, release date: 2004-11-23, Last modification date: 2023-08-23)
Primary citationGajiwala, K.S.,Pinko, C.
Structural rearrangement accompanying NAD+ synthesis within a bacterial DNA ligase crystal.
STRUCTURE, 12:1449-1459, 2004
Cited by
PubMed Abstract: DNA ligase is an enzyme important for DNA repair and replication. Eukaryotic genomes encode ligases requiring ATP as the cofactor; bacterial genomes encode NAD(+)-dependent ligase. This difference in substrate specificities and the essentiality of NAD(+)-dependent ligase for bacterial survival make NAD(+)-dependent ligase a good target for designing highly specific anti-infectives. Any such structure-guided effort would require the knowledge of the precise mechanism of NAD+ recognition by the enzyme. We report the principles of NAD+ recognition by presenting the synthesis of NAD+ from nicotinamide mononucleotide (NMN) and AMP, catalyzed by Enterococcus faecalis ligase within the crystal lattice. Unprecedented conformational change, required to reorient the two subdomains of the protein for the condensation to occur and to recognize NAD+, is captured in two structures obtained using the same protein crystal. Structural data and sequence analysis presented here confirms and extends prior functional studies of the ligase adenylation reaction.
PubMed: 15296738
DOI: 10.1016/j.str.2004.05.017
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

226707

數據於2024-10-30公開中

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