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

• KUNISHIMA Naoki

  Advanced Protein Crystallography Research Group, RIKEN SPring-8 Center, Harima Institute

Bibliographic Information

Other Title

• ビオチンプロテインリガーゼの結晶構造から見えたビオチンの活性化
• サイキン ノ ケンキュウ カラ ビオチンプロテインリガーゼ ノ ケッショウ コウゾウ カラ ミエタ ビオチン ノ カッセイカ

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.

Journal

• Nihon Kessho Gakkaishi

  Nihon Kessho Gakkaishi 48 (5), 354-358, 2006

  The Crystallographic Society of Japan

Details

• CRID: 1390282679064037760
• NII Article ID: 10018331303
• NII Book ID: AN00188364
• DOI: 10.5940/jcrsj.48.354
• ISSN: 18845576
• ISSN: 03694585
• NDL BIB ID: 8564073
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I8564073
• Text Lang: ja
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed