Crystal structure of the carboxy-terminal region of the bacteriophage T4 proximal long tail fiber protein Gp34

DOI: 10.3390/v9070168

Authors: Meritxell Granell (Centro Nacional de Biotecnologia (CNB-CSIC)) , Mikiyoshi Namura (Tokyo Institute of Technology) , Sara Alvira (Centro Nacional de Biotecnologia (CNB-CSIC); Universidad de Santiago de Compostela) , Shuji Kanamaru (Tokyo Institute of Technology) , Mark Van Raaij (Centro Nacional de Biotecnologia (CNB-CSIC); Universidad de Santiago de Compostela)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Viruses , VOL 9

State: Published (Approved)
Published: June 2017
Diamond Proposal Number(s): 5860

Abstract: Long tail fibers of bacteriophage T4 are formed by proteins gp34, gp35, gp36, and gp37, with gp34 located at the phage-proximal end and gp37 at the phage-distal, receptor-binding end. We have solved the structure of the carboxy-terminal region of gp34, consisting of amino acids 894–1289, by single-wavelength anomalous diffraction and extended the structure to amino acids 744–1289 using data collected from crystals containing longer gp34-fragments. The structure reveals three repeats of a mixed α-β fibrous domain in residues 744 to 877. A triple-helical neck connects to an extended triple β-helix domain (amino acids 900–1127) punctuated by two β-prism domains. Next, a β-prism domain decorated with short helices and extended β-helices is present (residues 1146–1238), while the C-terminal end is capped with another short β-helical region and three β-hairpins. The structure provides insight into the stability of the fibrous gp34 protein.

Journal Keywords: bacterial viruses; Caudovirales; Myoviridae; crystallography; fibrous protein

Diamond Keywords: Bacteriophages

Subject Areas: Biology and Bio-materials


Instruments: I04-Macromolecular Crystallography

Other Facilities: ESRF; DESY; ALBA

Added On: 24/07/2017 12:07

Documents:
viruses-09-00168.pdf

Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)