2VNL

MUTANT Y108Wdel OF THE HEADBINDING DOMAIN OF PHAGE P22 TAILSPIKE C- TERMINally fused to ISOLEUCINE ZIPPER pIIGCN4 (chimera II)

Summary for 2VNL

• Entry DOI: 10.2210/pdb2vnl/pdb
• Related: 1CLW 1LKT 1QA1 1QA2 1QA3 1QQ1 1QRB 1QRC 1TSP 1TYV 2VFM 2VFN 2VFO 2VFP 2VFQ 2VKY 2XC1
• Descriptor: BIFUNCTIONAL TAIL PROTEIN, PIIGCN4, GLYCEROL (3 entities in total)
• Functional Keywords: chimera, hydrolase, late protein, viral protein, phage p22 tailspike protein, mutant y108wdel, head-binding domain, isoleucine zipper piigcn4
• Biological source: ENTEROBACTERIA PHAGE P22 (SALMONELLA PHAGE P22); More
• Total number of polymer chains: 1
• Total formula weight: 17160.37

Authors

Mueller, J.J.,Seul, A.,Mueller, G.,Seckler, R.,Heinemann, U. (deposition date: 2008-02-05, release date: 2009-02-10, Last modification date: 2023-12-13)

Primary citation

Seul, A.,Mueller, J.J.,Andres, D.,Stettner, E.,Heinemann, U.,Seckler, R.
Bacteriophage P22 Tailspike: Structure of the Complete Protein and Function of the Interdomain Linker
Acta Crystallogr.,Sect.D, 70:1336-, 2014

PubMed Abstract: Attachment of phages to host cells, followed by phage DNA ejection, represents the first stage of viral infection of bacteria. Salmonella phage P22 has been extensively studied, serving as an experimental model for bacterial infection by phages. P22 engages bacteria by binding to the sugar moiety of lipopolysaccharides using the viral tailspike protein for attachment. While the structures of the N-terminal particle-binding domain and the major receptor-binding domain of the tailspike have been analyzed individually, the three-dimensional organization of the intact protein, including the highly conserved linker region between the two domains, remained unknown. A single amino-acid exchange in the linker sequence made it possible to crystallize the full-length protein. Two crystal structures of the linker region are presented: one attached to the N-terminal domain and the other present within the complete tailspike protein. Both retain their biological function, but the mutated full-length tailspike displays a retarded folding pathway. Fitting of the full-length tailspike into a published cryo-electron microscopy map of the P22 virion requires an elastic distortion of the crystal structure. The conservation of the linker suggests a role in signal transmission from the distal tip of the molecule to the phage head, eventually leading to DNA ejection.

PubMed: 24816102
DOI: 10.1107/S1399004714002685

Experimental method

X-RAY DIFFRACTION (1.8 Å)