2AKQ

The structure of bovine B-lactoglobulin A in crystals grown at very low ionic strength

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2AKQ の概要

• エントリーDOI: 10.2210/pdb2akq/pdb
• 関連するPDBエントリー: 1beb 1bso 3blg
• 分子名称: Beta-lactoglobulin variant A (2 entities in total)
• 機能のキーワード: b-lactoglbulin, crystal lattice, low ionic strength, pseudo-merohedral twinning, transport protein
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Secreted: P02754
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 73549.06

構造登録者

Adams, J.J.,Anderson, B.F.,Norris, G.E.,Creamer, L.K.,Jameson, G.B. (登録日: 2005-08-03, 公開日: 2005-08-16, 最終更新日: 2024-10-23)

主引用文献

Adams, J.J.,Anderson, B.F.,Norris, G.E.,Creamer, L.K.,Jameson, G.B.
Structure of bovine beta-lactoglobulin (variant A) at very low ionic strength
J.Struct.Biol., 154:246-254, 2006

PubMed Abstract: Bovine beta-lactoglobulin (BLG) is a globular protein of uncertain physiological function and a member of the lipocalin superfamily of proteins. Here, we present the X-ray structure at 3.0 angstroms of BLG (variant A) from an orthorhombic (P2(1)2(1)2(1)) pseudo-tetragonal crystal form that suffers from pseudo-merohedral twinning (final R(working) = 0.224, R(free) = 0.265). Crystals were grown by dialysis against ultra-purified water (i.e., at very low ionic strength), at pH approximately 5.2 (approximately pI), conditions vastly different from all other BLG structures determined previously. This allows critical assessment of the BLG structure and of the influence that pH, ionic strength, and crystal packing may have on the molecular structure of BLG. The pH-sensitive EF loop is found in the closed conformation characteristic of BLG at pH less than 7 and moderate to high ionic strength. Although the hydrophobic pocket appears to be empty, the presence of highly disordered water molecules cannot be excluded. The dimer interface and the hydrophobic pocket (calyx) are preserved. However, the orientation of the subunits in the dimer varies considerably with crystal form. Structure is deposited with PDB ID 2akq.

PubMed: 16540345
DOI: 10.1016/j.jsb.2005.12.010

実験手法

X-RAY DIFFRACTION (3 Å)