2LIG

THREE-DIMENSIONAL STRUCTURES OF THE LIGAND-BINDING DOMAIN OF THE BACTERIAL ASPARTATE RECEPTOR WITH AND WITHOUT A LIGAND

2LIG の概要

• エントリーDOI: 10.2210/pdb2lig/pdb
• 分子名称: ASPARTATE RECEPTOR, SULFATE ION, ASPARTIC ACID, ... (5 entities in total)
• 機能のキーワード: chemotaxis
• 由来する生物種: Salmonella typhimurium
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P02941
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37248.30

構造登録者

Kim, S.-H.,Yeh, J.I.,Prive, G.G.,Milburn, M.,Scott, W.,Koshland Junior, D.E. (登録日: 1995-04-18, 公開日: 1995-09-15, 最終更新日: 2024-10-23)

主引用文献

Milburn, M.V.,Prive, G.G.,Milligan, D.L.,Scott, W.G.,Yeh, J.,Jancarik, J.,Koshland Jr., D.E.,Kim, S.H.
Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand.
Science, 254:1342-1347, 1991

PubMed Abstract: The three-dimensional structure of an active, disulfide cross-linked dimer of the ligand-binding domain of the Salmonella typhimurium aspartate receptor and that of an aspartate complex have been determined by x-ray crystallographic methods at 2.4 and 2.0 angstrom (A) resolution, respectively. A single subunit is a four-alpha-helix bundle with two long amino-terminal and carboxyl-terminal helices and two shorter helices that form a cylinder 20 A in diameter and more than 70 A long. The two subunits in the disulfide-bonded dimer are related by a crystallographic twofold axis in the apo structure, but by a noncrystallographic twofold axis in the aspartate complex structure. The latter structure reveals that the ligand binding site is located more than 60 A from the presumed membrane surface and is at the interface of the two subunits. Aspartate binds between two alpha helices from one subunit and one alpha helix from the other in a highly charged pocket formed by three arginines. The comparison of the apo and aspartate complex structures shows only small structural changes in the individual subunits, except for one loop region that is disordered, but the subunits appear to change orientation relative to each other. The structures of the two forms of this protein provide a step toward understanding the mechanisms of transmembrane signaling.

PubMed: 1660187

実験手法

X-RAY DIFFRACTION (2 Å)