1Z6H

Solution Structure of Bacillus subtilis BLAP biotinylated-form

1Z6H の概要

• エントリーDOI: 10.2210/pdb1z6h/pdb
• NMR情報: BMRB: 6599
• 分子名称: Biotin/Lipoyl Attachment Protein, 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL (2 entities in total)
• 機能のキーワード: bacillus subtilis, single-domain biotin/lipoyl attachment protein, solution structure, biosynthetic protein
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8148.40

構造登録者

Cui, G.,Xia, B. (登録日: 2005-03-22, 公開日: 2006-03-22, 最終更新日: 2022-03-02)

主引用文献

Cui, G.,Nan, B.,Hu, J.,Wang, Y.,Jin, C.,Xia, B.
Identification and solution structures of a single domain biotin/lipoyl attachment protein from Bacillus subtilis
J.Biol.Chem., 281:20598-20607, 2006

PubMed Abstract: Protein biotinylation and lipoylation are post-translational modifications, in which biotin or lipoic acid is covalently attached to specific proteins containing biotin/lipoyl attachment domains. All the currently reported natural proteins containing biotin/lipoyl attachment domains are multidomain proteins and can only be modified by either biotin or lipoic acid in vivo. We have identified a single domain protein with 73 amino acid residues from Bacillus subtilis strain 168, and it can be both biotinylated and lipoylated in Escherichia coli. The protein is therefore named as biotin/lipoyl attachment protein (BLAP). This is the first report that a natural single domain protein exists as both a biotin and lipoic acid receptor. The solution structure of apo-BLAP showed that it adopts a typical fold of biotin/lipoyl attachment domain. The structure of biotinylated BLAP revealed that the biotin moiety is covalently attached to the side chain of Lys(35), and the bicyclic ring of biotin is folded back and immobilized on the protein surface. The biotin moiety immobilization is mainly due to an interaction between the biotin ureido ring and the indole ring of Trp(12). NMR study also indicated that the lipoyl group of the lipoylated BLAP is also immobilized on the protein surface in a similar fashion as the biotin moiety in the biotinylated protein.

PubMed: 16699181
DOI: 10.1074/jbc.M602660200

実験手法

SOLUTION NMR