Structural highlights
Publication Abstract from PubMed
The hemolymph of the fifth instar larvae of the silkworm Bombyx mori contains a group of homologous proteins with a molecular weight of approximately 30kDa, termed B. mori low molecular weight lipoproteins (Bmlps), which account for about 5% of the total plasma proteins. These so-called "30K proteins" have been reported to be involved in the innate immune response and transportation of lipid and/or sugar. To elucidate their molecular functions, we determined the crystal structure of a 30K protein, Bmlp7, at 1.91A. It has two distinct domains: an all-alpha N-terminal domain (NTD) and an all-beta C-terminal domain (CTD) of the beta-trefoil fold. Comparative structural analysis indicates that Bmlp7 represents a new family, adding to the 14 families currently identified, of the beta-trefoil superfamily. Structural comparison and simulation suggest that the NTD has a putative lipid-binding cavity, whereas the CTD has a potential sugar-binding site. However, we were unable to detect the binding of either lipid or sugar. Therefore, further investigations are needed to characterize the molecular function of this protein.
Crystal structure of the 30K protein from the silkworm Bombyx mori reveals a new member of the beta-trefoil superfamily.,Yang JP, Ma XX, He YX, Li WF, Kang Y, Bao R, Chen Y, Zhou CZ J Struct Biol. 2011 Jul;175(1):97-103. Epub 2011 Apr 14. PMID:21514389[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yang JP, Ma XX, He YX, Li WF, Kang Y, Bao R, Chen Y, Zhou CZ. Crystal structure of the 30K protein from the silkworm Bombyx mori reveals a new member of the beta-trefoil superfamily. J Struct Biol. 2011 Jul;175(1):97-103. Epub 2011 Apr 14. PMID:21514389 doi:10.1016/j.jsb.2011.04.003
