1IUD

MALTODEXTRIN-BINDING PROTEIN INSERTION/DELETION MUTANT WITH AN INSERTED B-CELL EPITOPE FROM THE PRES2 REGION OF HEPATITIS B VIRUS

Summary for 1IUD

• Entry DOI: 10.2210/pdb1iud/pdb
• Related PRD ID: PRD_900001
• Descriptor: MALTODEXTRIN-BINDING PROTEIN MALE-B133, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• Functional Keywords: pres2 epitope antigen virus, viral epitope insertion, hybrid protein, sugar transport
• Biological source: Escherichia coli
• Cellular location: Periplasm: P02928
• Total number of polymer chains: 1
• Total formula weight: 42149.50

Authors

Saul, F.A.,Vulliez-Le Normand, B.,Lema, F.,Bentley, G.A. (deposition date: 1996-05-29, release date: 1997-06-05, Last modification date: 2024-04-03)

Primary citation

Saul, F.A.,Vulliez-le Normand, B.,Lema, F.,Bentley, G.A.
Crystal structure of a recombinant form of the maltodextrin-binding protein carrying an inserted sequence of a B-cell epitope from the preS2 region of hepatitis B virus.
Proteins, 27:1-8, 1997

PubMed Abstract: We report the crystal structure of MalE-B133, a recombinant form of the maltodextrin-binding protein (MBP) of Escherichia coli carrying an inserted amino-acid sequence of a B-cell epitope from the preS2 region of the hepatitis B virus (HBV). The structure was determined by molecular replacement methods and refined to 2.7 A resolution. MalE-B133 is an insertion/deletion mutant of MBP in which residues from positions 134 to 142, an external alpha helix in the wild-type structure, are replaced by a foreign peptide segment of 19 amino acids. The inserted residues correspond to the preS2 sequence from positions 132 to 145 and five flanking residues that arise from the creation of restriction sites. The conformation of the recombinant protein, excluding the inserted segment, closely resembles that of wild-type MBP in the closed maltose-bound form. MalE-B133 was shown by previous studies to display certain immunogenic and antigenic properties of the hepatitis B surface antigen (HBsAg), which contains the preS2 region. The crystal structure reveals the conformation of the first nine epitope residues (preS2 positions 132 to 140) exposed on the surface of the molecule. The remaining five epitope residues (preS2 positions 141 to 145) are not visible in electron density maps. The path of the polypeptide chain in the visible portion of the insert differs from that of the deleted segment in the structure of wild-type MBP, displaying a helical conformation at positions 134 to 140 (preS2 sequence numbering). A tripeptide (Asp-Pro-Arg) at the N terminus of the helix forms a stable structural motif that may be implicated in the cross-reactivity of anti-HBsAg antibodies with the hybrid protein.

PubMed: 9037707
DOI: 10.1002/(SICI)1097-0134(199701)27:1<1::AID-PROT2>3.0.CO;2-L

Experimental method

X-RAY DIFFRACTION (2.7 Å)