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4UXF

Crystal structure of the carboxy-terminal region of the bacteriophage T4 proximal long tail fibre protein gp34, P21 native crystal

Summary for 4UXF
Entry DOI10.2210/pdb4uxf/pdb
Related4UXE 4UXG
DescriptorLARGE TAIL FIBER PROTEIN P34, GLYCEROL (3 entities in total)
Functional Keywordsviral protein, caudovirales, myoviridae, triple beta-helix
Biological sourceENTEROBACTERIA PHAGE T4
Cellular locationVirion : P18771
Total number of polymer chains3
Total formula weight134324.58
Authors
Granell, M.,Alvira, S.,Garcia-Doval, C.,Singh, A.K.,van Raaij, M.J. (deposition date: 2014-08-22, release date: 2015-12-16, Last modification date: 2024-05-08)
Primary citationGranell, M.,Namura, M.,Alvira, S.,Kanamaru, S.,van Raaij, M.J.
Crystal Structure of the Carboxy-Terminal Region of the Bacteriophage T4 Proximal Long Tail Fiber Protein Gp34.
Viruses, 9:-, 2017
Cited by
PubMed 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 -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.
PubMed: 28665339
DOI: 10.3390/v9070168
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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