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PDBsum entry 1z6h
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Biosynthetic protein
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PDB id
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1z6h
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References listed in PDB file
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Key reference
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Title
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Identification and solution structures of a single domain biotin/lipoyl attachment protein from bacillus subtilis.
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Authors
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G.Cui,
B.Nan,
J.Hu,
Y.Wang,
C.Jin,
B.Xia.
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Ref.
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J Biol Chem, 2006,
281,
20598-20607.
[DOI no: ]
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PubMed id
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Abstract
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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.
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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.
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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.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2006,
281,
20598-20607)
copyright 2006.
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