Journal
VIRUSES-BASEL
Volume 9, Issue 7, Pages -Publisher
MDPI AG
DOI: 10.3390/v9070168
Keywords
bacterial viruses; Caudovirales; Myoviridae; crystallography; fibrous protein
Categories
Funding
- Japanese Society for the Promotion of Science KAKENHI [JP25440066]
- Juan de la Cierva Fellowship from the Spanish Ministry of Economy, Industry and Competitiveness
- European Commission [NMP4-CT-2006-033256]
- [BFU2008-01588]
- [BFU2011-24843]
- [BFU2014-53425-P]
- [BFU2014-61367-EXP]
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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 alpha-beta fibrous domain in residues 744 to 877. A triple-helical neck connects to an extended triple beta-helix domain (amino acids 900-1127) punctuated by two beta-prism domains. Next, a beta-prism domain decorated with short helices and extended beta-helices is present (residues 1146-1238), while the C-terminal end is capped with another short beta-helical region and three beta-hairpins. The structure provides insight into the stability of the fibrous gp34 protein.
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