This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

5nxh

From Proteopedia

Jump to: navigation, search

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

Structural highlights

5nxh is a 3 chain structure with sequence from Escherichia virus T4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.89Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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