Baseplate structural protein gp6, C-terminal domain III
Baseplate structural protein gp6 is located next to the tail tube and is an intermediate (or inner) baseplate protein involved in tail assembly. Two molecules of gp6 form a complex with gp25 and gp7 which is involved sheath contraction [1-3]. This do ...
Baseplate structural protein gp6 is located next to the tail tube and is an intermediate (or inner) baseplate protein involved in tail assembly. Two molecules of gp6 form a complex with gp25 and gp7 which is involved sheath contraction [1-3]. This domain has been described as C-terminal domain III.
Baseplate structural protein gp6, C-terminal domain I
Baseplate structural protein gp6 is located next to the tail tube and is an intermediate (or inner) baseplate protein involved in tail assembly. Two molecules of gp6 form a complex with gp25 and gp7 which is involved sheath contraction [1-3]. This do ...
Baseplate structural protein gp6 is located next to the tail tube and is an intermediate (or inner) baseplate protein involved in tail assembly. Two molecules of gp6 form a complex with gp25 and gp7 which is involved sheath contraction [1-3]. This domain has been described as C-terminal domain I, and adopts a 2-layer beta-sandwich fold.
Baseplate structural protein gp6, C-terminal domain II
This entry represents domain II found in the C-terminal of gp6 from bacteriophage T4, which adopts a beta-barrel fold. This protein is involved in tail assembly. It forms the gp25-(gp6)2-gp7 module, involved in sheath contraction [1,2].
This domain is found in Baseplate wedge protein gp6 from Enterobacteria phage T4 and similar sequences predominantly from tailed bacteriophages. Gp6 is a protein involved in tail assembly. This entry represents the first part of Domain II [1].
This domain is found in Baseplate wedge protein gp6 from Enterobacteria phage T4 and similar sequences predominantly from tailed bacteriophages. Gp6 is a protein involved in tail assembly. This entry represents its N-terminal helical domain [1].
Baseplate structural protein Gp10, C-terminal domain
This entry represents the C-terminal domain (CTD) of baseplate structural protein Gp10 that assembles into trimeric structures. The core structure and assembly of Gp10 has structural similarity to that of the head domain of Gp11 and the receptor bind ...
This entry represents the C-terminal domain (CTD) of baseplate structural protein Gp10 that assembles into trimeric structures. The core structure and assembly of Gp10 has structural similarity to that of the head domain of Gp11 and the receptor binding domain of Gp12 [1]. The monomeric CTD of Gp10 consists of an alpha-helix followed by a three-stranded, antiparallel beta-sheet, which is almost perpendicular to the helix. The three symmetry related beta-sheets interact with their first beta-strands in the trimer, thus creating a flower-like arrangement with the alpha-helices being the flower stem and the three beta-sheets being the petals.
This entry represents the N-terminal domain of Baseplate protein gp9 from Bacteriophage T4, a component of the viral baseplate [1]. Gp9 connects the long tail fibres of the virus to the baseplate and triggers tail contraction after viral attachment t ...
This entry represents the N-terminal domain of Baseplate protein gp9 from Bacteriophage T4, a component of the viral baseplate [1]. Gp9 connects the long tail fibres of the virus to the baseplate and triggers tail contraction after viral attachment to a host cell. The protein is active as a trimer, with each monomer being composed of three domains. The N-terminal domain consists of an extended polypeptide chain and two alpha helices. The alpha1 helix from each of the three monomers in the trimer interacts with its counterparts to form a coiled-coil structure. The middle domain is a seven-stranded beta-sandwich. This entry represents the region including these two domains. Noticeably, the long flexible region between N-terminal and middle domains may be required for the function of gp9 to transmit signals from the long tail fibres [2]. Together with gp11, gp10 initiates the assembly of wedges that then go on to associate with a hub to form the viral baseplate [1].
This entry represents the N-terminal domain of Baseplate protein gp9 from Bacteriophage T4, a component of the viral baseplate [1]. Gp9 connects the long tail fibres of the virus to the baseplate and triggers tail contraction after viral attachment t ...
This entry represents the N-terminal domain of Baseplate protein gp9 from Bacteriophage T4, a component of the viral baseplate [1]. Gp9 connects the long tail fibres of the virus to the baseplate and triggers tail contraction after viral attachment to a host cell. The protein is active as a trimer, with each monomer being composed of three domains. The N-terminal domain consists of an extended polypeptide chain and two alpha helices. The alpha1 helix from each of the three monomers in the trimer interacts with its counterparts to form a coiled-coil structure. The middle domain is a seven-stranded beta-sandwich. This entry represents the region including these two domains. Noticeably, the long flexible region between N-terminal and middle domains may be required for the function of gp9 to transmit signals from the long tail fibres [2]. Together with gp11, gp10 initiates the assembly of wedges that then go on to associate with a hub to form the viral baseplate [1].
Members of this family of viral baseplate structural proteins adopt a structure consisting of a three-layer beta-sandwich with two finger-like loops containing an alpha-helix at the opposite sides of the sandwich. The two peripheral, five-stranded, a ...
Members of this family of viral baseplate structural proteins adopt a structure consisting of a three-layer beta-sandwich with two finger-like loops containing an alpha-helix at the opposite sides of the sandwich. The two peripheral, five-stranded, antiparallel beta-sheets are stacked against the middle, four-stranded, antiparallel beta-sheet. Attachment of this family of proteins to the baseplate during assembly creates a binding site for subsequent attachment of Gp6 [1].
This family represents T4 phage gp25 protein and gp25-like proteins, found in several systems, including contractile tail bacteriophages, the type VI secretion system (T6SS) and R-type pyocins, which constitute a multiprotein tubular apparatus to att ...
This family represents T4 phage gp25 protein and gp25-like proteins, found in several systems, including contractile tail bacteriophages, the type VI secretion system (T6SS) and R-type pyocins, which constitute a multiprotein tubular apparatus to attach to and penetrate host cell membranes. Gp25 is a component of the conserved wedge in the inner part of the baseplate and serves as a nucleus for sheath polymerisation, playing a critical role in sheath assembly and contraction [1,2]. The EPR motif (Glu-Pro-Arg, residues 85-87 of gp25) is conserved across all members of the family including orthologues from the RpoS-mediated general stress response system (called IraD) [3,4]. This motif interacts with the 'core bundle' composed of orthologues of T4 gp6 and gp7 proteins in contractile injection systems.
Members of this family adopt a beta barrel structure with a Greek key topology, which is topologically similar to the FMN-binding split barrel. They are structural component of the viral baseplate, predominantly found in the structural protein gp27 [ ...
Members of this family adopt a beta barrel structure with a Greek key topology, which is topologically similar to the FMN-binding split barrel. They are structural component of the viral baseplate, predominantly found in the structural protein gp27 [1].
Members of this family adopt a beta barrel structure with a Greek key topology, which is topologically similar to the FMN-binding split barrel. They are structural component of the viral baseplate, predominantly found in the structural protein gp27 [ ...
Members of this family adopt a beta barrel structure with a Greek key topology, which is topologically similar to the FMN-binding split barrel. They are structural component of the viral baseplate, predominantly found in the structural protein gp27 [1].
This domain is found at the N terminus of the Gp5 baseplate protein of bacteriophage T4. This domain binds to the Gp27 protein [1]. This domain has the common OB fold [1].
This domain is found in Baseplate wedge protein gp7 from Bacteriophage T4 and similar proteins predominantly found in tailed bacteriophages. Gp7 provides the primary control of the conformational changes of the viral baseplate during assembly and inf ...
This domain is found in Baseplate wedge protein gp7 from Bacteriophage T4 and similar proteins predominantly found in tailed bacteriophages. Gp7 provides the primary control of the conformational changes of the viral baseplate during assembly and infection. This protein is organised into six domains connected by flexible linkers. This entry represents helix-turn-helix motif that is part of the long linker connecting the second and fourth domains [1].
This domain is found in Baseplate wedge protein gp7 from Bacteriophage T4 and similar proteins predominantly found in tailed bacteriophages. Gp7 provides the primary control of the conformational changes of the viral baseplate during assembly and inf ...
This domain is found in Baseplate wedge protein gp7 from Bacteriophage T4 and similar proteins predominantly found in tailed bacteriophages. Gp7 provides the primary control of the conformational changes of the viral baseplate during assembly and infection. This protein is organised into six domains connected by flexible linkers. This entry represents Domain V, which is an insertion into domain IV and consists of an eight-stranded beta- barrel followed by two short alpha-helices [1].
This domain is found in Baseplate wedge protein gp7 from Bacteriophage T4 and similar proteins predominantly found in tailed bacteriophages. Gp7 provides the primary control of the conformational changes of the viral baseplate during assembly and inf ...
This domain is found in Baseplate wedge protein gp7 from Bacteriophage T4 and similar proteins predominantly found in tailed bacteriophages. Gp7 provides the primary control of the conformational changes of the viral baseplate during assembly and infection. This protein is organised into six domains connected by flexible linkers. This entry represents Domain VI, which forms a ribbon-like structure that interacts with N-terminal region of the protein Gp10 [1].
Members of this family of viral baseplate structural proteins adopt a structure consisting of a three-layer beta-sandwich with two finger-like loops containing an alpha-helix at the opposite sides of the sandwich. The two peripheral, five-stranded, a ...
Members of this family of viral baseplate structural proteins adopt a structure consisting of a three-layer beta-sandwich with two finger-like loops containing an alpha-helix at the opposite sides of the sandwich. The two peripheral, five-stranded, antiparallel beta-sheets are stacked against the middle, four-stranded, antiparallel beta-sheet. Attachment of this family of proteins to the baseplate during assembly creates a binding site for subsequent attachment of Gp6 [1].
This entry represents the N-terminal domain of Baseplate protein gp9 from Bacteriophage T4, a component of the viral baseplate [1]. Gp9 connects the long tail fibres of the virus to the baseplate and triggers tail contraction after viral attachment t ...
This entry represents the N-terminal domain of Baseplate protein gp9 from Bacteriophage T4, a component of the viral baseplate [1]. Gp9 connects the long tail fibres of the virus to the baseplate and triggers tail contraction after viral attachment to a host cell. The protein is active as a trimer, with each monomer being composed of three domains. The N-terminal domain consists of an extended polypeptide chain and two alpha helices. The alpha1 helix from each of the three monomers in the trimer interacts with its counterparts to form a coiled-coil structure. The middle domain is a seven-stranded beta-sandwich. This entry represents the region including these two domains. Noticeably, the long flexible region between N-terminal and middle domains may be required for the function of gp9 to transmit signals from the long tail fibres [2]. Together with gp11, gp10 initiates the assembly of wedges that then go on to associate with a hub to form the viral baseplate [1].
