3PUB
Crystal structure of the Bombyx mori low molecular weight lipoprotein 7 (Bmlp7)
Summary for 3PUB
| Entry DOI | 10.2210/pdb3pub/pdb |
| Descriptor | 30kDa protein (2 entities in total) |
| Functional Keywords | beta-trefoil fold, haemolymph, unknown function |
| Biological source | Bombyx mori (silk moth, silkworm) |
| Total number of polymer chains | 2 |
| Total formula weight | 57929.27 |
| Authors | Yang, J.-P.,Ma, X.-X.,He, Y.-X.,Li, W.-F.,Kang, Y.,Bao, R.,Chen, Y.,Zhou, C.-Z. (deposition date: 2010-12-03, release date: 2011-06-01, Last modification date: 2024-03-20) |
| Primary citation | Yang, J.-P.,Ma, X.-X.,He, Y.-X.,Li, W.-F.,Kang, Y.,Bao, R.,Chen, Y.,Zhou, C.-Z. Crystal structure of the 30 K protein from the silkworm Bombyx mori reveals a new member of the beta-trefoil superfamily J.Struct.Biol., 175:97-103, 2011 Cited by PubMed Abstract: The hemolymph of the fifth instar larvae of the silkworm Bombyx mori contains a group of homologous proteins with a molecular weight of approximately 30 kDa, termed B. mori low molecular weight lipoproteins (Bmlps), which account for about 5% of the total plasma proteins. These so-called "30 K 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 30 K protein, Bmlp7, at 1.91Å. It has two distinct domains: an all-α N-terminal domain (NTD) and an all-β C-terminal domain (CTD) of the β-trefoil fold. Comparative structural analysis indicates that Bmlp7 represents a new family, adding to the 14 families currently identified, of the β-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. PubMed: 21514389DOI: 10.1016/j.jsb.2011.04.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.91 Å) |
Structure validation
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