1Z6H

Solution Structure of Bacillus subtilis BLAP biotinylated-form

Summary for 1Z6H

• Entry DOI: 10.2210/pdb1z6h/pdb
• NMR Information: BMRB: 6599
• Descriptor: Biotin/Lipoyl Attachment Protein, 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL (2 entities in total)
• Functional Keywords: bacillus subtilis, single-domain biotin/lipoyl attachment protein, solution structure, biosynthetic protein
• Biological source: Bacillus subtilis
• Total number of polymer chains: 1
• Total formula weight: 8148.40

Authors

Cui, G.,Xia, B. (deposition date: 2005-03-22, release date: 2006-03-22, Last modification date: 2022-03-02)

Primary citation

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

Experimental method

SOLUTION NMR