1OX3

crystal structure of mini-fibritin

Summary for 1OX3

• Entry DOI: 10.2210/pdb1ox3/pdb
• Descriptor: Fibritin (2 entities in total)
• Functional Keywords: foldon, capping motif, chaperone
• Biological source: Enterobacteria phage T4; More
• Cellular location: Virion : P10104
• Total number of polymer chains: 1
• Total formula weight: 11914.26

Authors

Boudko, S.P.,Stetefeld, J. (deposition date: 2003-04-01, release date: 2004-04-13, Last modification date: 2023-08-16)

Primary citation

Boudko, S.P.,Strelkov, S.V.,Engel, J.,Stetefeld, J.
Design and Crystal Structure of Bacteriophage T4 Mini-Fibritin NCCF.
J.Mol.Biol., 339:927-935, 2004

PubMed Abstract: Fibritin is a fibrous protein that forms "whiskers" attached to the neck of bacteriophage T4. Whiskers interact with the long tail fibers regulating the assembly and infectivity of the virus. The fibritin trimer includes the N-terminal domain responsible for attachment to the phage particle and for the collar formation, the central domain forming a 500 A long segmented coiled-coil structure, and the C-terminal "foldon" domain. We have designed a "mini" fibritin with most of the coiled-coil domain deleted, and solved its crystal structure. The non-helical N-terminal part represents a new protein fold that tightly interacts with the coiled-coil segment forming a single domain, as revealed by calorimetry. The analysis of the crystal structure and earlier electron microscopy data on the collar-whisker complex suggests the necessity of other proteins to participate in the collar formation. Crystal structure determination of the N-terminal domain of fibritin is the first step towards elucidating the detailed structure and assembly mechanism of the collar-whisker complex.

PubMed: 15165860
DOI: 10.1016/j.jmb.2004.04.001

Experimental method

X-RAY DIFFRACTION (2 Å)