3ct5

Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail

spinqualitylabelsall models 3ct5, resolution 1.37Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ct5 is a 1 chain structure with sequence from Bacteriophage phi-29. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAG Related: 3csq, 3csr, 3csz, 3ct0, 3ct1 Gene: 13 (Bacteriophage phi-29) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [VG13_BPPH2] Essential for tail assembly and the production of infectious particles. Degrades the peptidoglycan layer of the host cell wall and thereby facilitates infection of host bacteria. Acts probably as multifunctional enzyme that degrades N-acetylglucosamine polymers (in vitro) and cleaves the peptide cross-links of the host cell wall (Probable). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail.,Xiang Y, Morais MC, Cohen DN, Bowman VD, Anderson DL, Rossmann MG Proc Natl Acad Sci U S A. 2008 Jul 15;105(28):9552-7. Epub 2008 Jul 7. PMID:18606992 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA