Structural highlights
Function
FIBP_BPT4 Structural component of the proximal-half of the long-tail fiber. The long-tail fibers of T4 are about 1600 Angstroms long with a kink in the middle that divides the fiber into proximal and distal halves.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cerritelli ME, Wall JS, Simon MN, Conway JF, Steven AC. Stoichiometry and domainal organization of the long tail-fiber of bacteriophage T4: a hinged viral adhesin. J Mol Biol. 1996 Aug 2;260(5):767-80. PMID:8709154 doi:http://dx.doi.org/10.1006/jmbi.1996.0436
- ↑ Granell M, Namura M, Alvira S, Kanamaru S, van Raaij MJ. Crystal Structure of the Carboxy-Terminal Region of the Bacteriophage T4 Proximal Long Tail Fiber Protein Gp34. Viruses. 2017 Jun 30;9(7). pii: E168. doi: 10.3390/v9070168. PMID:28665339 doi:http://dx.doi.org/10.3390/v9070168
