1tae: Difference between revisions

Revision as of 06:12, 29 July 2008

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File:1tae.png

Template:STRUCTURE 1tae

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

Template:ABSTRACT PUBMED 15296738

About this StructureAbout this Structure

1TAE is a Single protein structure of sequence from Enterococcus faecalis v583. Full crystallographic information is available from OCA.

ReferenceReference

Structural rearrangement accompanying NAD+ synthesis within a bacterial DNA ligase crystal., Gajiwala KS, Pinko C, Structure. 2004 Aug;12(8):1449-59. PMID:15296738

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OCA

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-'''Structural rearrangement accompanying NAD+ synthesis within a bacterial DNA ligase crystal'''
+===Structural rearrangement accompanying NAD+ synthesis within a bacterial DNA ligase crystal===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15296738}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15296738}}
 ==About this Structure==
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 [[Category: Pinko, C.]]
 [[Category: Nucleotidyl transferase fold]]
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