3CT0
Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail
3CT0 の概要
エントリーDOI | 10.2210/pdb3ct0/pdb |
関連するPDBエントリー | 3CSQ 3CSR 3CSZ 3CT1 3CT5 |
分子名称 | Morphogenesis protein 1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
機能のキーワード | cell wall, phi29, hydrolase, infection, late protein |
由来する生物種 | Bacteriophage phi-29 |
細胞内の位置 | Virion : P15132 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 19271.53 |
構造登録者 | |
主引用文献 | Xiang, Y.,Morais, M.C.,Cohen, D.N.,Bowman, V.D.,Anderson, D.L.,Rossmann, M.G. Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail. Proc.Natl.Acad.Sci.Usa, 105:9552-9557, 2008 Cited by PubMed Abstract: The small bacteriophage phi29 must penetrate the approximately 250-A thick external peptidoglycan cell wall and cell membrane of the Gram-positive Bacillus subtilis, before ejecting its dsDNA genome through its tail into the bacterial cytoplasm. The tail of bacteriophage phi29 is noncontractile and approximately 380 A long. A 1.8-A resolution crystal structure of gene product 13 (gp13) shows that this tail protein has spatially well separated N- and C-terminal domains, whose structures resemble lysozyme-like enzymes and metallo-endopeptidases, respectively. CryoEM reconstructions of the WT bacteriophage and mutant bacteriophages missing some or most of gp13 shows that this enzyme is located at the distal end of the phi29 tail knob. This finding suggests that gp13 functions as a tail-associated, peptidoglycan-degrading enzyme able to cleave both the polysaccharide backbone and peptide cross-links of the peptidoglycan cell wall. Comparisons of the gp13(-) mutants with the phi29 mature and emptied phage structures suggest the sequence of events that occur during the penetration of the tail through the peptidoglycan layer. PubMed: 18606992DOI: 10.1073/pnas.0803787105 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.77 Å) |
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