Visualization of Biotin Activation Through a Comparison of Crystal Structures of Biotin Protein Ligase

Accession number;06A0976109
Title;Visualization of Biotin Activation Through a Comparison of Crystal Structures of Biotin Protein Ligase
Author; KUNISHIMA NAOKI (Inst. Physical and Chemical Res., JPN)
Journal Title;Journal of the Crystallographic Society of Japan
Journal Code:G0232A
ISSN:0369-4585
VOL.48;NO.5;PAGE.354-358(2006)
Figure&Table&Reference;FIG.5, REF.8
Pub. Country;Japan
Language;Japanese
Abstract;Biotin protein ligase(BPL)catalyses the synthesis of an activated form of biotin, biotinyl-5'-AMP, from substrates biotin and ATP followed by biotinylation of the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase. In order to visualize the structural feature of the BPL reaction, crystal structures of BPL from Pyrococcus horikoshii OT3 have been determined in an unliganded form and three liganded forms with biotin, ADP and the reaction intermediate biotinyl-5'-AMP. The exact locations of the ligands and the active site residues allow us to propose a general scheme for the first step of the reaction carried out by BPL. (author abst.)