4IY8
Bmlp3 - P21 crystal form
Summary for 4IY8
| Entry DOI | 10.2210/pdb4iy8/pdb |
| Related | 3PUB 4EFP 4EFQ 4EFR 4IY9 |
| Descriptor | 30K protein 1, HEXAETHYLENE GLYCOL, DI(HYDROXYETHYL)ETHER, ... (4 entities in total) |
| Functional Keywords | lipoprotein 11 family, hemolymph, lipid binding protein |
| Biological source | Bombyx mori (silk moth,silkworm) |
| Total number of polymer chains | 4 |
| Total formula weight | 110840.78 |
| Authors | Pietrzyk, A.J.,Bujacz, A.,Mueller-Dieckmann, J.,Jaskolski, M.,Bujacz, G. (deposition date: 2013-01-28, release date: 2013-04-24, Last modification date: 2023-09-20) |
| Primary citation | Pietrzyk, A.J.,Bujacz, A.,Mueller-Dieckmann, J.,Lochynska, M.,Jaskolski, M.,Bujacz, G. Two Crystal Structures of Bombyx mori Lipoprotein 3 - Structural Characterization of a New 30-kDa Lipoprotein Family Member. Plos One, 8:e61303-e61303, 2013 Cited by PubMed Abstract: The 30-kDa family of lipoproteins from insect hemolymph has been the focus of a number of studies over the last few years. Recently, four crystal structures of Bombyx mori lipoprotein 7 have been determined. Here we report two crystal structures of another member of the 30-kDa lipoprotein family, Bombyx mori lipoprotein 3 (Bmlp3). The protein was isolated from its natural source, mulberry silkworm hemolymph. It crystallized in two different crystal forms, Bmlp3-p21 (space group P21) and Bmlp3-c2 (space group C2). The crystal structures were solved by molecular replacement using the coordinates of Bmlp7 as a starting model. The crystals of Bmlp3-p21 diffracted X-rays to 2.4 Å resolution and of Bmlp3-c2 to 2.1 Å resolution. Bmlp3 has an overall fold characteristic of 30-kDa lipoproteins, with a VHS-type N-terminal domain and β-trefoil C-terminal domain. Structural comparison of Bmlp3 and Bmlp7 shows that the loops present in the C-terminal domain are flexible and participate in dimer formation. Additionally, new putative binding sites of Bmlp3 have been analyzed in detail and the electrostatic potential of the protein surface at physiological pH 7.4 conditions has been calculated. The results of these calculations are the starting point for an explanation of the recently reported cell-penetrating properties of the 30-kDa lipoproteins. PubMed: 23613829DOI: 10.1371/journal.pone.0061303 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.36 Å) |
Structure validation
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