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

Agnieszka J Pietrzyk; Anna Bujacz; Malgorzata Łochynska; Mariusz Jaskolski; Grzegorz Bujacz

doi:10.1371/journal.pone.0108761

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

PLoS One. 2014 Nov 7;9(11):e108761. doi: 10.1371/journal.pone.0108761. eCollection 2014.

Authors

Agnieszka J Pietrzyk¹, Anna Bujacz², Malgorzata Łochynska³, Mariusz Jaskolski⁴, Grzegorz Bujacz⁵

Affiliations

¹ Center for Biocrystallographic Research, Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland.
² Institute of Technical Biochemistry, Faculty of Biotechnology and Food Sciences, Technical University of Lodz, Lodz, Poland.
³ Institute of Natural Fibers and Medicinal Plants, Poznan, Poland.
⁴ Center for Biocrystallographic Research, Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland; Department of Crystallography, Faculty of Chemistry, A. Mickiewicz University, Poznan, Poland.
⁵ Center for Biocrystallographic Research, Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland; Institute of Technical Biochemistry, Faculty of Biotechnology and Food Sciences, Technical University of Lodz, Lodz, Poland.

Abstract

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.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Animals
Bombyx*
Crystallography, X-Ray
Databases, Protein
Hemolymph
Insect Proteins / chemistry*
Lipoproteins / chemistry*
Models, Molecular
Molecular Sequence Data
Molecular Weight
Protein Folding
Protein Structure, Tertiary
Sequence Alignment

Substances

Insect Proteins
Lipoproteins

Grants and funding

This work was supported in part by the European Union within the European Regional Development Fund and by grant 2011/03/B/NZ1/01238 from the National Science Centre to GB. The use of the BESSY and the DESY beamlines received funding from the European Community's Seventh Framework Programme (FP7/2007-2013) under BioStruct-X (grant agreement No. 283570). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.