4PC4
Bombyx mori lipoprotein 6
Summary for 4PC4
| Entry DOI | 10.2210/pdb4pc4/pdb |
| Related | 3PUB 4EFP 4EFQ 4EFR 4IY8 4IY9 |
| Descriptor | 30K lipoprotein, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, 1,2-ETHANEDIOL, ... (6 entities in total) |
| Functional Keywords | 30-kda lipoprotein, hemolymph, lipid binding protein |
| Biological source | Bombyx mori (Silk moth) |
| Total number of polymer chains | 5 |
| Total formula weight | 142945.99 |
| Authors | Pietrzyk, A.J.,Bujacz, A.,Jaskolski, M.,Bujacz, G. (deposition date: 2014-04-14, release date: 2015-03-04, Last modification date: 2024-11-13) |
| Primary citation | Pietrzyk, A.J.,Bujacz, A.,ochynska, M.,Jaskolski, M.,Bujacz, G. Crystal structure of Bombyx mori lipoprotein 6: comparative structural analysis of the 30-kDa lipoprotein family. Plos One, 9:e108761-e108761, 2014 Cited by PubMed 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. PubMed: 25379889DOI: 10.1371/journal.pone.0108761 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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