Crystal structure of Bombyx mori lipoprotein 6: comparative structural analysis of the 30-kDa lipoprotein family

The 30-kDa lipoprotein (LP) family of mulberry silkworm comprises major hemolymph proteins specific to the fifth instar larvae. The family consists of 46 members, 24 of which are referred to as typical 30-kDa LPs. To date, two crystal structures of 30-kDa LPs from Bombyx mori have been described (Bm...

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Bibliographic Details
Published in:PloS one 2014-11, Vol.9 (11), p.e108761-e108761
Main Authors: Pietrzyk, Agnieszka J, Bujacz, Anna, Łochynska, Malgorzata, Jaskolski, Mariusz, Bujacz, Grzegorz
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Automation
Biochemistry
Biology and Life Sciences
Bombyx
Bombyx mori
Cell culture
Chromatography
Conformation
Crystal structure
Crystallography
Crystallography, X-Ray
Databases, Protein
Electrostatic properties
Genomes
Genomics
Hemolymph
Insect Proteins - chemistry
Larvae
Lipoproteins
Lipoproteins - chemistry
Models, Molecular
Molecular Sequence Data
Molecular Weight
Physiological aspects
Physiology
Protein Folding
Protein Structure, Tertiary
Proteins
Sequence Alignment
Structural analysis
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Summary:The 30-kDa lipoprotein (LP) family of mulberry silkworm comprises major hemolymph proteins specific to the fifth instar larvae. The family consists of 46 members, 24 of which are referred to as typical 30-kDa LPs. To date, two crystal structures of 30-kDa LPs from Bombyx mori have been described (Bmlp3 and Bmlp7). Here, we present the crystal structure of Bmlp6, another 30-kDa LP member. Bmlp6 is comprised of two domains characteristic of this family, the VHS-type N-terminal domain and β-trefoil C-terminal domain. The structures of the three 30-kDa LPs have been compared and a number of differences are noted, including loop conformation, the surface electrostatic potential, and the potential binding cavities. We discuss the observed structural differences in the light of the potential different roles of the particular 30-kDa LP members in silkworm physiology.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0108761