4NLI
Crystal structure of sheep beta-lactoglobulin (space group P3121)
4NLI の概要
| エントリーDOI | 10.2210/pdb4nli/pdb |
| 関連するPDBエントリー | 4nlj |
| 分子名称 | Beta-lactoglobulin-1/B, SULFATE ION (3 entities in total) |
| 機能のキーワード | lipocalin, transport, milk, transport protein |
| 由来する生物種 | Ovis aries (domestic sheep,lambs,wild sheep) |
| 細胞内の位置 | Secreted: P67976 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 18581.37 |
| 構造登録者 | Loch, J.I.,Molenda, M.,Kopec, M.,Swiatek, S.,Lewinski, K. (登録日: 2013-11-14, 公開日: 2014-03-12, 最終更新日: 2024-10-30) |
| 主引用文献 | Loch, J.I.,Molenda, M.,Kopec, M.,Swiatek, S.,Lewinski, K. Structure of two crystal forms of sheep beta-lactoglobulin with EF-loop in closed conformation Biopolymers, 101:886-894, 2014 Cited by PubMed Abstract: Ovine β-lactoglobulin has been isolated from whey fraction of sheep milk and crystallized. The high-resolution structures of two crystal forms (triclinic and trigonal) obtained at pH 7.0 have been determined revealing that ovine protein, similarly to its bovine analog, is dimeric. Access to the binding site located in the eight-stranded antiparallel β-barrel in both structures is blocked by the EF loop that has been found in closed conformation. Similarly to bovine lactoglobulin (BLG), conformation of the EF loop is stabilized by hydrogen bond between Glu89 and Ser116 indicating that Tanford transition might occur with the same mechanism. The substitution at six positions in relation to the most abundant isoform B of BLG also affects the distribution of electrostatic potentials and the total charge. PubMed: 25098178DOI: 10.1002/bip.22471 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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