PDBsum entry 1d0n

Contractile protein

PDB id: 1d0n

Contents

Protein chains

729 a.a. *

Waters ×284

* Residue conservation analysis

PDB id:

1d0n

Name:

Contractile protein

Title:

The crystal structure of calcium-free equine plasma gelsolin.

Structure:

Horse plasma gelsolin. Chain: a, b

Source:

Equus caballus. Horse. Organism_taxid: 9796. Tissue: plasma

Biol. unit:

Dimer (from PQS)

Resolution:

2.50Å R-factor: 0.205 R-free: 0.238

Authors:

L.D.Burtnick,R.Robinson,C.Li

Key ref:

L.D.Burtnick et al. (1997). The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation. Cell, 90, 661-670. PubMed id: 9288746 DOI: 10.1016/S0092-8674(00)80527-9

Date:

13-Sep-99 Release date: 15-Sep-99

Protein chains

Q28372  (GELS_HORSE) -  Gelsolin from Equus caballus

Seq: 731 a.a.

Struc: 729 a.a.

DOI no: 10.1016/S0092-8674(00)80527-9

Cell 90:661-670 (1997)

PubMed id: 9288746

The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation.

L.D.Burtnick, E.K.Koepf, J.Grimes, E.Y.Jones, D.I.Stuart, P.J.McLaughlin, R.C.Robinson.

ABSTRACT

The structure of gelsolin has been determined by crystallography and comprises six structurally related domains that, in a Ca2+-free environment, pack together to form a compact globular structure in which the putative actin-binding sequences are not sufficiently exposed to enable binding to occur. We propose that binding Ca2+ can release the connections that join the N- and C-terminal halves of gelsolin, enabling each half to bind actin relatively independently. Domain shifts are proposed in response to Ca2+ as bases for models of how gelsolin acts to sever, cap, or nucleate F-actin filaments. The structure also invites discussion of polyphosphoinositide binding to segment 2 and suggests how mutation at Asp-187 could initiate a series of events that lead to deposition of amyloid plaques, as observed in victims of familial amyloidosis (Finnish type).

Selected figure(s)

Figure 1.
Figure 1. The Structure of Gelsolin(A) Schematic representations of the six domains of gelsolin in similar orientations. A standard coloring of the segments is used here and in subsequent figures: S1, red; S2, light green; S3, yellow; S4, pink; S5, dark green; and S6, orange.(B) The relative organization of S1–S3 and S4–S6. The schematic representation shows S1–S3 (upper panel) and S4–S6 (lower panel) in approximately the same orientation. Linker regions are striped with the colors of the linked segments.(C) Schematic representations of the structure of whole gelsolin. The upper panel shows a view rotated by 90° clockwise around the horizontal with respect to the lower panel. The C-terminal extension is striped orange and black.

Figure 2.
Figure 2. The Topology of GelsolinThe topology of gelsolin. β strands are depicted as arrows and helices as rectangles.

The above figures are reprinted by permission from Cell Press: Cell (1997, 90, 661-670) copyright 1997.

Figures were selected by an automated process.