2VBM

Tailspike protein of bacteriophage Sf6 complexed with tetrasaccharide

Summary for 2VBM

• Entry DOI: 10.2210/pdb2vbm/pdb
• Related: 2VBE 2VBK
• Descriptor: TAILSPIKE-PROTEIN, alpha-L-rhamnopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-L-rhamnopyranose-(1-2)-alpha-L-rhamnopyranose, PHOSPHATE ION, ... (6 entities in total)
• Functional Keywords: viral adhesion protein, viral protein, hydrolase, tailspike, endorhamnosidase, right-handed parallel beta-helix
• Biological source: ENTEROBACTERIA PHAGE SF6
• Total number of polymer chains: 1
• Total formula weight: 56016.17

Authors

Mueller, J.J.,Barbirz, S.,Freiberg, A.,Seckler, R.,Heinemann, U. (deposition date: 2007-09-14, release date: 2008-04-22, Last modification date: 2023-12-13)

Primary citation

Muller, J.J.,Barbirz, S.,Heinle, K.,Freiberg, A.,Seckler, R.,Heinemann, U.
An Intersubunit Active Site between Supercoiled Parallel Beta Helices in the Trimeric Tailspike Endorhamnosidase of Shigella Flexneri Phage Sf6.
Structure, 16:766-, 2008

PubMed Abstract: Sf6 belongs to the Podoviridae family of temperate bacteriophages that infect gram-negative bacteria by insertion of their double-stranded DNA. They attach to their hosts specifically via their tailspike proteins. The 1.25 A crystal structure of Shigella phage Sf6 tailspike protein (Sf6 TSP) reveals a conserved architecture with a central, right-handed beta helix. In the trimer of Sf6 TSP, the parallel beta helices form a left-handed, coiled-beta coil with a pitch of 340 A. The C-terminal domain consists of a beta sandwich reminiscent of viral capsid proteins. Further crystallographic and biochemical analyses show a Shigella cell wall O-antigen fragment to bind to an endorhamnosidase active site located between two beta-helix subunits each anchoring one catalytic carboxylate. The functionally and structurally related bacteriophage, P22 TSP, lacks sequence identity with Sf6 TSP and has its active sites on single subunits. Sf6 TSP may serve as an example for the evolution of different host specificities on a similar general architecture.

PubMed: 18462681
DOI: 10.1016/J.STR.2008.01.019

Experimental method

X-RAY DIFFRACTION (2 Å)