Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 105, Issue 28, Page 9552-9557, Year 2008
Publish date	Jul 15, 2008
Authors	Ye Xiang / Marc C Morais / Daniel N Cohen / Valorie D Bowman / Dwight L Anderson / Michael G Rossmann /
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 ...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.
External links	Proc Natl Acad Sci U S A / PubMed:18606992 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	1.37 - 35.0 Å
Structure data	EMDB-1506: Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail Method: EM (single particle) / Resolution: 30.0 Å EMDB-5010: Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail Method: EM (single particle) / Resolution: 35.0 Å PDB-3csq: Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail Method: X-RAY DIFFRACTION / Resolution: 1.8 Å PDB-3csr: Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail Method: X-RAY DIFFRACTION / Resolution: 1.8 Å PDB-3csz: Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail Method: X-RAY DIFFRACTION / Resolution: 1.8 Å PDB-3ct0: Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail Method: X-RAY DIFFRACTION / Resolution: 1.77 Å PDB-3ct1: Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail Method: X-RAY DIFFRACTION / Resolution: 1.51 Å PDB-3ct5: Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail Method: X-RAY DIFFRACTION / Resolution: 1.37 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-HOH: WATER / Water
Source	bacteriophage phi-29 (virus)
Keywords	HYDROLASE / infection / phi29 / Late protein / cell wall