The shapes and sizes of two domains of tropomodulin, the P-end-capping protein of actin-tropomyosin.

Abstract:

:Tropomodulin, the P-end (slow-growing end)-capping protein of the actin-tropomyosin filament, and its fragment (C20) of the C-terminal half were studied by synchrotron small-angle X-ray scattering, restoring low-resolution shapes using an ab initio shape-determining procedure. Tropomodulin is elongated (115 A long) and consists of two domains, one of 65 A in length and the other being similar to C20 in shape and size if the long axes of the two are tilted by about 40 degrees relative to each other. We propose a model for tropomodulin in association with tropomyosin and actin: the N-terminal half of tropomodulin, a rod, binds to the N-terminus of tropomyosin and the C-terminal triangle domain protrudes from the P-end being slightly bent towards the actin subunit at the end, thereby blocking the P-end.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Fujisawa T,Kostyukova A,Maéda Y

doi

10.1016/s0014-5793(01)02498-x

keywords:

subject

Has Abstract

pub_date

2001-06-01 00:00:00

pages

67-71

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(01)02498-X

journal_volume

498

pub_type

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