2CHD

Crystal structure of the C2A domain of Rabphilin-3A

2CHD の概要

• エントリーDOI: 10.2210/pdb2chd/pdb
• 関連するPDBエントリー: 1ZBD 3RPB
• 分子名称: RABPHILIN-3A, GLYCEROL (3 entities in total)
• 機能のキーワード: rabphilin-3a, c2 domain, c2a, calcium binding, synaptic exocytosis, metal-binding, protein transport, synapse, transport, zinc-finger
• 由来する生物種: RATTUS NORVEGICUS (RAT)
• 細胞内の位置: Cell junction, synapse : P47709
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16308.41

構造登録者

Biadene, M.,Montaville, P.,Sheldrick, G.M.,Becker, S. (登録日: 2006-03-14, 公開日: 2006-06-28, 最終更新日: 2023-12-13)

主引用文献

Biadene, M.,Montaville, P.,Sheldrick, G.M.,Becker, S.
Structure of the C2A Domain of Rabphilin-3A.
Acta Crystallogr.,Sect.D, 62:793-, 2006

PubMed Abstract: Rabphilin-3A is a neuronal protein containing a C2-domain tandem. To date, only the structure of the C2B domain has been solved. The crystal structure of the Ca2+-free C2A domain has been solved by molecular replacement and refined to 1.92 A resolution. It adopts the classical C2-domain fold consisting of an eight-stranded antiparallel beta-sandwich with type I topology. In agreement with its Ca2+-dependent negatively charged membrane-binding properties, this C2 domain contains all the conserved acidic residues responsible for calcium binding. However, the replacement of a conserved aspartic acid residue by glutamic acid allows formation of an additional strong hydrogen bond, resulting in increased rigidity of calcium-binding loop 1. The electrostatic surface of the C2A domain consists of a large positively charged belt surrounded by two negatively charged patches located at both tips of the domain. In comparison, the structurally very similar C2A domain of synaptotagmin I has a highly acidic electrostatic surface, suggesting completely unrelated functions for these two C2A domains.

PubMed: 16790935
DOI: 10.1107/S0907444906017537

実験手法

X-RAY DIFFRACTION (1.92 Å)