1SVY

SEVERIN DOMAIN 2, 1.75 ANGSTROM CRYSTAL STRUCTURE

1SVY の概要

• エントリーDOI: 10.2210/pdb1svy/pdb
• 分子名称: SEVERIN, CALCIUM ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: actin-binding protein, calcium-binding, cytoskeleton, gelsolin, severin, villin, calcium, pip2
• 由来する生物種: Dictyostelium discoideum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12339.91

構造登録者

Puius, Y.A.,Fedorov, E.V.,Eichinger, L.,Sullivan, M.,Schleicher, M.,Almo, S.C. (登録日: 1998-08-10, 公開日: 1999-08-10, 最終更新日: 2024-06-05)

主引用文献

Puius, Y.A.,Fedorov, E.V.,Eichinger, L.,Schleicher, M.,Almo, S.C.
Mapping the functional surface of domain 2 in the gelsolin superfamily.
Biochemistry, 39:5322-5331, 2000

PubMed Abstract: The crystal structure of the F-actin binding domain 2 of severin, the gelsolin homologue from Dictyostelium discoideum, has been determined by multiple isomorphous replacement and refined to 1.75 A resolution. The structure reveals an alpha-helix-beta-sheet sandwich similar to the domains of gelsolin and villin, and contains two cation-binding sites, as observed in other domain 1 and domain 2 homologues. Comparison of the structures of several gelsolin family domains has identified residues that may mediate F-actin binding in gelsolin domain 2 homologues. To assess the involvement of these residues in F-actin binding, three mutants of human gelsolin domain 2 were assayed for F-actin binding activity and thermodynamic stability. Two of the mutants, RRV168AAA and RLK210AAA, demonstrated a lowered affinity for F-actin, indicating a role for those residues in filament binding. Using both structural and biochemical data, we have constructed a model of the gelsolin domain 1-domain 2-F-actin complex. This model highlights a number of interactions that may serve as positive and negative determinants of filament end- and side-binding.

PubMed: 10820002
DOI: 10.1021/bi992364d

実験手法

X-RAY DIFFRACTION (1.75 Å)