 |
PDBsum entry 4bql
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Contractile protein
|
PDB id
|
|
|
|
4bql
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structure of crenactin, An archaeal actin homologue active at 90°c.
|
|
|
Authors
|
|
A.C.Lindås,
M.Chruszcz,
R.Bernander,
K.Valegård.
|
|
|
Ref.
|
|
Acta Crystallogr D Biol Crystallogr, 2014,
70,
492-500.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The crystal structure of the archaeal actin, crenactin, from the rod-shaped
hyperthermophilic (optimal growth at 90°C) crenarchaeon Pyrobaculum
calidifontis is reported at 3.35 Å resolution. Despite low amino-acid
sequence identity, the three-dimensional structure of the protein monomer is
highly similar to those of eukaryotic actin and the bacterial MreB protein.
Crenactin-specific features are also evident, as well as elements that are
shared between crenactin and eukaryotic actin but are not found in MreB. In the
crystal, crenactin monomers form right-handed helices, demonstrating that the
protein is capable of forming filament-like structures. Monomer interactions in
the helix, as well as interactions between crenactin and ADP in the
nucleotide-binding pocket, are resolved at the atomic level and compared with
those of actin and MreB. The results provide insights into the structural and
functional properties of a heat-stable archaeal actin and contribute to the
understanding of the evolution of actin-family proteins in the three domains of
life.
|
|
|
|
|
|
|
