PDBsum entry 1z6h

Biosynthetic protein

PDB id: 1z6h

Contents

Protein chain

72 a.a. *

Ligands

BTI

* Residue conservation analysis

PDB id:

1z6h

Name:

Biosynthetic protein

Title:

Solution structure of bacillus subtilis blap biotinylated-form

Structure:

Biotin/lipoyl attachment protein. Chain: a. Engineered: yes

Source:

Bacillus subtilis. Organism_taxid: 1423. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

G.Cui,B.Xia

Key ref:

G.Cui et al. (2006). Identification and solution structures of a single domain biotin/lipoyl attachment protein from Bacillus subtilis. J Biol Chem, 281, 20598-20607. PubMed id: 16699181 DOI: 10.1074/jbc.M602660200

Date:

22-Mar-05 Release date: 22-Mar-06

Protein chain

C0H419  (BLAP_BACSU) -  Biotin/lipoyl attachment protein from Bacillus subtilis (strain 168)

Seq: 73 a.a.

Struc: 72 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1074/jbc.M602660200

J Biol Chem 281:20598-20607 (2006)

PubMed id: 16699181

Identification and solution structures of a single domain biotin/lipoyl attachment protein from Bacillus subtilis.

G.Cui, B.Nan, J.Hu, Y.Wang, C.Jin, B.Xia.

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.

Selected figure(s)

Figure 3.
FIGURE 3. Solution structure of btl-BLAP. A, superimposition of 20 representative structures of btl-BLAP (stereo view). The regular secondary structure regions are in red, and the loops/coils are in cyan. The target lysine (magenta) and the attached biotin (green) are also shown. B, superimposition of the mean structures of apo-(blue) and btl-BLAP (red) in ribbon diagram. The target lysine in apo-BLAP (blue) and the biotin-attached lysine (red) in btl-BLAP are shown. C, electrostatic surface of btl-BLAP. Biotin moiety is displayed in yellow.

Figure 4.
FIGURE 4. Comparison of structures of apo-BLAP (A), btl-BLAP (B), E. coli BCCP (1BDO) (C), and 1.3 S subunit (D) (1DCZ). The side chains of residues affected by the biotinylation in BLAP are shown in magenta. The side chains of corresponding residues in other proteins are also shown. The side chain of the target lysine is displayed in yellow, and the biotin is displayed in blue.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2006, 281, 20598-20607) copyright 2006.

Figures were selected by the author.