4OMW
Crystal structure of goat beta-lactoglobulin (orthorhombic form)
Summary for 4OMW
| Entry DOI | 10.2210/pdb4omw/pdb |
| Related | 4OMX |
| Descriptor | Beta-lactoglobulin, GLYCEROL, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | lipocalin, transport, transport protein |
| Biological source | Capra hircus (domestic goat, goats) |
| Cellular location | Secreted: P02756 |
| Total number of polymer chains | 4 |
| Total formula weight | 73677.60 |
| Authors | Loch, J.I.,Swiatek, S.,Czub, M.,Ludwikowska, M.,Lewinski, K. (deposition date: 2014-01-27, release date: 2014-11-19, Last modification date: 2024-11-20) |
| Primary citation | Loch, J.I.,Bonarek, P.,Polit, A.,Swiatek, S.,Czub, M.,Ludwikowska, M.,Lewinski, K. Conformational variability of goat beta-lactoglobulin: Crystallographic and thermodynamic studies. Int.J.Biol.Macromol., 72C:1283-1291, 2014 Cited by PubMed Abstract: Goat β-lactoglobulin (GLG), lipocalin protein sharing high sequence similarity to bovine β-lactoglobulin (BLG), has been structurally and thermodynamically characterized. Two crystal forms of GLG have been obtained, trigonal (P3121) and orthorhombic (P21212), with unique molecular packing, not observed previously for BLG. In the trigonal structure, GLG molecules have EF-loop in closed conformation while in the orthorhombic structure, for the first time, symmetric and asymmetric dimers of β-lactoglobulin are observed simultaneously. It indicates that the opening or closing EF-loop does not occur in both subunits at the same time but might be sequential and cooperative. Comparison of GLG and BLG structures revealed presence of various conformers of EF and GH. ITC studies showed that at pH 7.5 GLG binds sodium dodecyl sulfate with Gibbs energy similar to BLG, however, with different contribution from enthalpic and entropic component. At pH 7.5 GLG forms dimers with dimerization constant Ka = 34.28 × 10(3) M(-1), significantly higher than observed for BLG. Similar mechanism of conformational changes and ligand binding indicates that GLG and BLG may play analogous biological role. PubMed: 25450833DOI: 10.1016/j.ijbiomac.2014.10.031 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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