TY - JOUR
T1 - The tail lysozyme complex of bacteriophage T4
AU - Arisaka, Fumio
AU - Kanamaru, Shuji
AU - Leiman, Petr
AU - Rossmann, Michael G.
N1 - Funding Information:
We thank Brian Matthews for hosting one of us (Shuji Kanamaru) during the early stages of this project. We thank the staff of BioCARS for their help and advice in the data collection at the Advanced Photon Source beam lines, 14-BM-C and 14-BM-D. The work was supported by a National Science Foundation Grant to M.G.R.; Grants-in-Aid for Scientific Research from the Ministry of Education, Science, Sports, and Culture of Japan to F.A.; and a reinvestment Grant from Purdue University.
PY - 2003/1/1
Y1 - 2003/1/1
N2 - The tail baseplate of bacteriophage T4 contains a structurally essential, three-domain protein encoded by gene 5 in which the middle domain possesses lysozyme activity. The gene 5 product (gp5) undergoes post-translational cleavage, allowing the resultant N-terminal domain (gp5*) to assemble into the baseplate as a trimer. The lysozyme activity of the undissociated cleaved gp5 is inhibited until infection has been initiated, when the C-terminal portion of the molecule is detached and the rest of the molecule dissociates into monomers. The 3D structure of the undissociated cleaved gp5, complexed with gp27 (another component of the baseplate), shows that it is a cell-puncturing device that functions to penetrate the outer cell membrane and to locally dissolve the periplasmic cell wall.
AB - The tail baseplate of bacteriophage T4 contains a structurally essential, three-domain protein encoded by gene 5 in which the middle domain possesses lysozyme activity. The gene 5 product (gp5) undergoes post-translational cleavage, allowing the resultant N-terminal domain (gp5*) to assemble into the baseplate as a trimer. The lysozyme activity of the undissociated cleaved gp5 is inhibited until infection has been initiated, when the C-terminal portion of the molecule is detached and the rest of the molecule dissociates into monomers. The 3D structure of the undissociated cleaved gp5, complexed with gp27 (another component of the baseplate), shows that it is a cell-puncturing device that functions to penetrate the outer cell membrane and to locally dissolve the periplasmic cell wall.
KW - Bacteriophage T4
KW - Genes 5 and 27
KW - Tail lysozyme complex
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U2 - 10.1016/S1357-2725(02)00098-5
DO - 10.1016/S1357-2725(02)00098-5
M3 - Short survey
C2 - 12467643
AN - SCOPUS:0037212295
SN - 1357-2725
VL - 35
SP - 16
EP - 21
JO - International Journal of Biochemistry and Cell Biology
JF - International Journal of Biochemistry and Cell Biology
IS - 1
ER -