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- W2732171239 endingPage "168" @default.
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- W2732171239 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." @default.
- W2732171239 created "2017-07-14" @default.
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- W2732171239 date "2017-06-30" @default.
- W2732171239 modified "2023-09-27" @default.
- W2732171239 title "Crystal Structure of the Carboxy-Terminal Region of the Bacteriophage T4 Proximal Long Tail Fiber Protein Gp34" @default.
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- W2732171239 doi "https://doi.org/10.3390/v9070168" @default.
- W2732171239 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5537660" @default.
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