From the first to the second domain of gelsolin: a common path on the surface of actin?1

FEBS Letters

Narayan, Kartik²  Burtnick, Leslie D.¹  Robinson, Robert C.²  Urosev, Dunja¹  Irobi, Edward² 

[1] Department of Chemistry and Center for Blood Research, University of British Columbia, Vancouver, BC, Canada V6T 1Z1;Department of Medical Biochemistry and Microbiology, Uppsala University, BMC, Box 582, 751 23 Uppsala, Sweden

关键词: Gelsolin;    Actin;    WH2 domain;    Crystal structure;    G1+;    human gelsolin fragment Met25 to Gln160;    G1;    gelsolin domain 1;    G2;    gelsolin domain 2;    WASp;    Wiscott–Aldridge syndrome protein;    WIP;    WASp interacting protein;    WH2;    WASp homology domain 2;    WAVE;    WASp family verprolin homologous protein;    CAP;    adenyl cyclase-associated protein;   

DOI  :  10.1016/S0014-5793(03)00934-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We present the 2.6 Å resolution crystal structure of a complex formed between G-actin and gelsolin fragment Met25–Gln160 (G1+). The structure differs from those of other gelsolin domain 1 (G1) complexes in that an additional six amino acid residues from the crucial linker region into gelsolin domain 2 (G2) are visible and are attached securely to the surface of actin. The linker segment extends away from G1 up the face of actin in a direction that infers G2 will bind along the same long-pitch helical strand as the actin bound to G1. This is consistent with a mechanism whereby G2 attaches gelsolin to the side of a filament and then directs G1 toward a position where it would disrupt actin–actin contacts. Alignment of the sequence of the structurally important residues within the G1–G2 linker with those of WH2 (WASp homology domain 2) domain protein family members (e.g. WASp (Wiscott–Aldridge syndrome protein) and thymosin β4) suggests that the opposing activities of filament assembly and disassembly may exploit a common patch on the surface of actin.

【 授权许可】

Unknown