4CJ7

Structure of Crenactin, an archeal actin-like protein

Summary for 4CJ7

• Entry DOI: 10.2210/pdb4cj7/pdb
• Descriptor: ACTIN/ACTIN FAMILY PROTEIN, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• Functional Keywords: structural protein, parm, archea, filament
• Biological source: PYROBACULUM CALIDIFONTIS
• Total number of polymer chains: 2
• Total formula weight: 97705.37

Authors

Izore, T.,Duman, R.E.,Kureisaite-Ciziene, D.,Lowe, J. (deposition date: 2013-12-19, release date: 2014-01-22, Last modification date: 2023-12-20)

Primary citation

Izore, T.,Duman, R.,Kureisaite-Ciziene, D.,Lowe, J.
Crenactin from Pyrobaculum Calidifontis is Closely Related to Actin in Structure and Forms Steep Helical Filaments.
FEBS Lett., 588:776-, 2014

PubMed Abstract: Polymerising proteins of the actin family are nearly ubiquitous. Crenactins, restricted to Crenarchaea, are more closely related to actin than bacterial MreB. Crenactins occur in gene clusters hinting at an unknown, but conserved function. We solved the crystal structure of crenactin at 3.2 Å resolution. The protein crystallises as a continuous right-handed helix with 8 subunits per complete turn, spanning 419 Å. The structure of crenactin shows several loops that are longer than in actin, but overall, crenactin is closely related to eukaryotic actin, with an RMSD of 1.6 Å. Crenactin filaments imaged by electron microscopy showed polymers with very similar helical parameters.

PubMed: 24486010
DOI: 10.1016/J.FEBSLET.2014.01.029

Experimental method

X-RAY DIFFRACTION (3.2 Å)