6K22

Crystal structure of Ca-bound human Annexin A5 in low salt condition

6K22 の概要

• エントリーDOI: 10.2210/pdb6k22/pdb
• 関連するPDBエントリー: 6K25
• 分子名称: Annexin A5, CALCIUM ION (3 entities in total)
• 機能のキーワード: annexin a5, phospholipid binding, membrane repair, anxa5, lipid binding protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37539.44

構造登録者

Hong, S.,Ha, N.-C. (登録日: 2019-05-13, 公開日: 2020-03-25, 最終更新日: 2023-11-22)

主引用文献

Hong, S.,Na, S.,Kim, O.H.,Jeong, S.,Oh, B.C.,Ha, N.C.
High-resolution structures of annexin A5 in a two-dimensional array.
J.Struct.Biol., 209:107401-107401, 2020

PubMed Abstract: Annexins are soluble cytosolic proteins that bind to cell membranes. Annexin A5 self-assembles into a two-dimensional (2D) array and prevents cell rupture by attaching to damaged membranes. However, this process is not fully understood at the molecular level. In this study, we determined the crystal structures of annexin A5 with and without calcium (Ca) and confirmed the Ca-dependent outward motion of a tryptophan residue. Strikingly, the two structures exhibited the same crystal packing and 2D arrangement into a p3 lattice, which agrees well with the results of low-resolution structural imaging. High-resolution structures indicated that a three-fold interaction near the tryptophan residue is important for mediating the formation of the p3 lattice. A hypothesis on the promotion of p3 lattice formation by phosphatidyl serine (PS) is also suggested. This study provides molecular insight into how annexins modulate the physical properties of cell membranes as a function of Ca concentration and the phospholipid composition of the membrane.

PubMed: 31605770
DOI: 10.1016/j.jsb.2019.10.003

実験手法

X-RAY DIFFRACTION (2.747 Å)