5NXH

Crystal structure of the carboxy-terminal region of the bacteriophage T4 proximal long tail fibre protein gp34, residues 744-1289 at 2.9 Angstrom resolution

Summary for 5NXH

• Entry DOI: 10.2210/pdb5nxh/pdb
• Descriptor: Long-tail fiber proximal subunit, GLYCEROL (3 entities in total)
• Functional Keywords: viral protein, caudovirales, myoviridae, structural protein
• Biological source: Enterobacteria phage T4
• Cellular location: Virion : P18771
• Total number of polymer chains: 3
• Total formula weight: 182537.39

Authors

Namura, M.,van Raaij, M.J.,Kanamaru, S. (deposition date: 2017-05-10, release date: 2017-07-12, Last modification date: 2024-01-17)

Primary citation

Granell, M.,Namura, M.,Alvira, S.,Kanamaru, S.,van Raaij, M.J.
Crystal Structure of the Carboxy-Terminal Region of the Bacteriophage T4 Proximal Long Tail Fiber Protein Gp34.
Viruses, 9:-, 2017

PubMed 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 -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.

PubMed: 28665339
DOI: 10.3390/v9070168

Experimental method

X-RAY DIFFRACTION (2.89 Å)