1P8Z

Complex Between Rabbit Muscle alpha-Actin: Human Gelsolin Residues Val26-Glu156

Summary for 1P8Z

• Entry DOI: 10.2210/pdb1p8z/pdb
• Descriptor: Gelsolin precursor, plasma, Actin, alpha skeletal muscle, CADMIUM ION, ... (6 entities in total)
• Functional Keywords: linker between gelsolin domain 1 and domain 2, structural protein-contractile protein complex, structural protein/contractile protein
• Biological source: Homo sapiens (human); More
• Cellular location: Isoform 2: Cytoplasm, cytoskeleton. Isoform 1: Secreted: P06396; Cytoplasm, cytoskeleton: P68135
• Total number of polymer chains: 2
• Total formula weight: 58284.72

Authors

Irobi, E.,Burtnick, L.D.,Robinson, R.C. (deposition date: 2003-05-08, release date: 2003-10-14, Last modification date: 2024-02-14)

Primary citation

Irobi, E.,Burtnick, L.D.,Urosev, D.,Narayan, K.,Robinson, R.C.
From the First to the second domain of gelsolin: A common path on the surface of actin?
FEBS lett., 552:86-90, 2003

PubMed Abstract: We present the 2.6 A 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 beta4) suggests that the opposing activities of filament assembly and disassembly may exploit a common patch on the surface of actin.

PubMed: 14527665
DOI: 10.1016/S0014-5793(03)00934-7

Experimental method

X-RAY DIFFRACTION (2.6 Å)