Sandbox Reserved 717: Difference between revisions

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Short tail fibres consist of the single protein gp12. This protein forms a parallel, in-register, homo-trimer of 527 residues per subunit. ~~'''~~18 monomers are on the baseplate.~~'''~~ 1ocy is a monomer of the short tail fibres. ~~'''~~A monomer of gp12 has a mass of 55.3 kDa.~~'''~~ ~~'''~~Gp12 N-terminal domain ~~attached it~~ to the baseplate. While the C-terminal globular domain is supposed to bind the bacterial host cell. ~~'''~~

Short tail fibres consist of the single protein gp12. This protein forms a parallel, in-register, homo-trimer of 527 residues per subunit. 18 monomers are on the baseplate. 1ocy is a monomer of the short tail fibres. A monomer of gp12 has a mass of 55.3 kDa. The Gp12 N-terminal domain is bound to the baseplate. While the C-terminal globular domain is supposed to bind the bacterial host cell.

Gp12 can be divided into two fragments. One ~~frgament~~ with a mass of 33kDA and a second with a mass of 45kDa.

Gp12 can be divided into two fragments. One fragment with a mass of 33kDA and a second with a mass of 45kDa.

==The 33kDa Fragment <ref>PMID: 12888344</ref> <ref>PMID:11530935</ref>==

The 33kDa (PDB:1H6W) ~~fragment~~ was generated in the presence of EDTA. This fragment contains the residues 85-395 and 518-527. The residues 397-517 are lacking because of internal deletion.

The 33kDa fragment (PDB:1H6W) was generated in the presence of EDTA. This fragment contains the residues 85-395 and 518-527. The residues 397-517 are lacking because of internal deletion.

The 33kDa fragment can be further sub-divided into two subunits. The neck (residue 333-341) and the collar (residues 342-396 plus 518-527). The neck connects the body of the fibre to its C-terminal collar and receptor binding-site. It consists of a triple alpha-helix of residues 333-341.

The 33kDa fragment can be further sub-divided into two subunits. The neck (residue 333-341) and the collar (residues 342-396 plus 518-527). The neck connects the body of the fibre to its C-terminal collar and receptor binding-site. It consists of a triple alpha-helix which is built by the residues 333-341.

The collar domain is a small globular domain. It contains six beta-strands and an alpha-helix.

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==Receptor-Binding Domain ==

Gp12 is fixed with its N-terminal domain to the baseplate. So the C-terminal domain has to be involved in LPS-binding. To detect where the receptor-binding domain is, full-length gp12, 33kDa fragments and 45kDa fragments were immobilised in micro-plate wells and were allowed to bind to bacteria[1]. The result was that the 33kDa fragment did never bind to a bacteria. The 45kDa fragment did bind. So the receptor-binding domain is absent in the 33kDa fragment but present in the 45kDa fragment. The residues which are present in the 45kDa fragment and lacking in the 33kDa fragment are the residues 397-517. They are referred to be the receptor-binding domain.

Gp12 is fixed with its N-terminal domain to the baseplate. So the C-terminal domain has to be involved in LPS-binding. To detect where the receptor-binding domain is, full-length gp12, 33kDa fragments and 45kDa fragments were immobilised in micro-plate wells and were allowed to bind to bacteria[1]. The result was that the 33kDa fragment did never bind to a bacteria. The 45kDa fragment did bind. So the receptor-binding domain is absent in the 33kDa fragment but present in the 45kDa fragment. The residues which are present in the 45kDa fragment and lacking in the 33kDa fragment are the residues 397-517. They are referred to be part of the receptor-binding domain.

Sandbox Reserved 717: Difference between revisions

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@@ Line 44: / Line 44: @@
 <Structure load='1ocy' size='500' frame='true' align='right' caption='1ocy' scene=' />
-Short tail fibres consist of the single protein gp12. This protein forms a parallel, in-register, homo-trimer of 527 residues per subunit. '''18 monomers are on the baseplate.''' 1ocy is a monomer of the short tail fibres. '''A monomer of gp12 has a mass of 55.3 kDa.'''  '''Gp12 N-terminal domain attached it to the baseplate. While the C-terminal globular domain is supposed to bind the bacterial host cell. '''
+Short tail fibres consist of the single protein gp12. This protein forms a parallel, in-register, homo-trimer of 527 residues per subunit. 18 monomers are on the baseplate. 1ocy is a monomer of the short tail fibres. A monomer of gp12 has a mass of 55.3 kDa.  The Gp12 N-terminal domain is bound to the baseplate. While the C-terminal globular domain is supposed to bind the bacterial host cell.
-Gp12 can be divided into two fragments. One frgament with a mass of 33kDA and a second with a mass of 45kDa.
+Gp12 can be divided into two fragments. One fragment with a mass of 33kDA and a second with a mass of 45kDa.
 ==The 33kDa Fragment <ref>PMID: 12888344</ref> <ref>PMID:11530935</ref>==
-The 33kDa (PDB:1H6W) fragment was generated in the presence of EDTA. This fragment contains the residues 85-395 and 518-527. The residues 397-517 are lacking because of internal deletion.
+The 33kDa fragment (PDB:1H6W)  was generated in the presence of EDTA. This fragment contains the residues 85-395 and 518-527. The residues 397-517 are lacking because of internal deletion.
-The 33kDa fragment can be further sub-divided into two subunits. The neck (residue 333-341) and the collar (residues 342-396 plus 518-527). The neck connects the body of the fibre to its C-terminal collar and receptor binding-site. It consists of a triple alpha-helix of residues 333-341.
+The 33kDa fragment can be further sub-divided into two subunits. The neck (residue 333-341) and the collar (residues 342-396 plus 518-527). The neck connects the body of the fibre to its C-terminal collar and receptor binding-site. It consists of a triple alpha-helix which is built by the residues 333-341.
 The collar domain is a small globular domain. It contains six beta-strands and an alpha-helix.
@@ Line 58: / Line 58: @@
 ==Receptor-Binding Domain ==
-Gp12 is fixed with its N-terminal domain to the baseplate. So the C-terminal domain has to be involved in LPS-binding. To detect where the receptor-binding domain is, full-length gp12, 33kDa fragments and 45kDa fragments were immobilised in micro-plate wells and were allowed to bind to bacteria[1]. The result was that the 33kDa fragment did never bind to a bacteria. The 45kDa fragment did bind. So the receptor-binding domain is absent in the 33kDa fragment but present in the 45kDa fragment. The residues which are present in the 45kDa fragment and lacking in the 33kDa fragment are the residues 397-517. They are referred to be the receptor-binding domain.
+Gp12 is fixed with its N-terminal domain to the baseplate. So the C-terminal domain has to be involved in LPS-binding. To detect where the receptor-binding domain is, full-length gp12, 33kDa fragments and 45kDa fragments were immobilised in micro-plate wells and were allowed to bind to bacteria[1]. The result was that the 33kDa fragment did never bind to a bacteria. The 45kDa fragment did bind. So the receptor-binding domain is absent in the 33kDa fragment but present in the 45kDa fragment. The residues which are present in the 45kDa fragment and lacking in the 33kDa fragment are the residues 397-517. They are referred to be part of the receptor-binding domain.