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Crystal structure of Bacillus subtilis SPP1 phage gp23.1, a putative chaperone. High-resolution structure.Crystal structure of Bacillus subtilis SPP1 phage gp23.1, a putative chaperone. High-resolution structure.
Structural highlights
FunctionPublication Abstract from PubMedSPP1 is a siphophage infecting the gram-positive bacterium Bacillus subtilis. The SPP1 tail EM reconstruction revealed that it is mainly constituted by conserved structural proteins such as the major tail proteins (MTPs, gp17.1), the tape measure protein (TMP, gp18), the Distal tail protein (Dit, gp19.1) and the Tail associated lysine (Tal, gp21). A group of 5 small genes (22-24.1) follows in the genome but it remains to be elucidated whether their protein products belong or not to the tail. Noteworthy, an unassigned EM density accounting for approximately 245 kDa is present at the distal end of the SPP1 tail-tip. We report here the gp23.1 crystal structure at 1.6 A resolution, a protein that lacks sequence identity to any known protein. We found that gp23.1 forms a hexamer both in the crystal lattice and in solution as revealed by light scattering measurements. The gp23.1 hexamer does not fit well in the unassigned SPP1 tail-tip EM density and we hypothesize that this protein might act as a chaperone. Crystal structure of Bacillus subtilis SPP1 phage gp23.1, a putative chaperone.,Veesler D, Blangy S, Lichiere J, Ortiz-Lombardia M, Tavares P, Campanacci V, Cambillau C Protein Sci. 2010 Jul 27. PMID:20665904[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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