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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| - | + | 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. | |
| - | + | Crystal Structure of the Carboxy-Terminal Region of the Bacteriophage T4 Proximal Long Tail Fiber Protein Gp34.,Granell M, Namura M, Alvira S, Kanamaru S, van Raaij MJ Viruses. 2017 Jun 30;9(7). pii: E168. doi: 10.3390/v9070168. PMID:28665339<ref>PMID:28665339</ref> | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Revision as of 16:35, 20 October 2017
Crystal structure of the carboxy-terminal region of the bacteriophage T4 proximal long tail fibre protein gp34, P21 selenomethionine crystal
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