Sandbox Reserved 717: Difference between revisions

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After the creation of six wedge composed of gp11, gp10, gp7, gp8, gp6, gp25 and gp53, is the wedge associated to the hub. The hub is a complex of gp5-gp27. Then are gp9 and gp12 added. The chaperone protein gp57 help gp12 to adopt its correct folding into trimmers. To finish, gp48 and gp54 are added and it form the complete baseplate.

== '''Structure''' ==

== '''Structure <ref> doi:10.1038/nsb970</ref>''' ==

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==Ligands and their Binding-Sites==

==1.)So4==

In the gp12 there are two molecules of SO4 ligands. One of them SO4 (1529) interacts with the citric acid.

The other SO4 molecule (1530) interacts with Ser387. It builds two hydrogen bounds to Ser287 with the distances 2.66 and 3.20.

==2.)citric acid==

The citric acid interacts with following amino acids: Arg465 (distance 3.01) and Asp455(distance 2.42). These interactions are caused by hydrogen bounds.

==3.)zinc==

The zinc is located in the centre of the receptor-binding domain. The zinc-binding site lies on the border between the head and the bonnet of the 45kDa domain. It interacts with the amino acids His445 and His447 of each monomer. The distances of the zinc ion to the NE2 of His445 and His447 ara 2.22 Å and 2.25 Å. The normally found distances between His and zinc are shorter. The explaination that these distances are longer than normally found is the octahedral coordination of the zinc in this structure.

The role of the zinc ion is probably absolute of structural nature. It increases the stability of the C-terminus of gp12 against proteases, but it also raises the stability of the C-terminus in general.

Sandbox Reserved 717: Difference between revisions

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@@ Line 40: / Line 40: @@
 After the creation of six wedge composed of gp11, gp10, gp7, gp8, gp6, gp25 and gp53, is the wedge associated to the hub. The hub is a complex of gp5-gp27. Then are gp9 and gp12 added. The chaperone protein gp57 help gp12 to adopt its correct folding into trimmers. To finish, gp48 and gp54 are added and it form the complete baseplate.
-== '''Structure''' ==
+== '''Structure <ref> doi:10.1038/nsb970</ref>'''  ==
 <Structure load='1ocy' size='500' frame='true' align='right' caption='1ocy' scene=' />
@@ Line 81: / Line 81: @@
 ==Ligands and their Binding-Sites==
 ==1.)So4==
+In the gp12 there are two molecules of SO4 ligands. One of them SO4 (1529) interacts with the citric acid.
+The other SO4 molecule (1530) interacts with Ser387. It builds two hydrogen bounds to Ser287 with the distances 2.66 and 3.20.
 ==2.)citric acid==
+The citric acid interacts with following amino acids: Arg465 (distance 3.01) and Asp455(distance 2.42). These interactions are caused by hydrogen bounds.
 ==3.)zinc==
+The zinc is located in the centre of the receptor-binding domain. The zinc-binding site lies on the border between the head and the bonnet of the 45kDa domain. It interacts with the amino acids His445 and His447 of each monomer. The distances of the zinc ion to the NE2 of His445 and His447 ara 2.22 Å and 2.25 Å. The normally found distances between His and zinc are shorter. The explaination that these distances are longer than normally found is the octahedral coordination of the zinc in this structure.
+The role of the zinc ion is probably absolute of structural nature. It increases the stability of the C-terminus of gp12 against proteases, but it also raises the stability of the C-terminus in general.