User:Ramiro Barrantes/FpgNeiRepair
From Proteopedia
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| <scene name='User:Ramiro_Barrantes/Workbench/Lys160asp178/1' target="fpg">Lys160 and Asp178</scene> | | <scene name='User:Ramiro_Barrantes/Workbench/Lys160asp178/1' target="fpg">Lys160 and Asp178</scene> | ||
| <scene name='User:Ramiro_Barrantes/Workbench/Econeiarginine171/1' target="ecoNei">Arg171</scene> | | <scene name='User:Ramiro_Barrantes/Workbench/Econeiarginine171/1' target="ecoNei">Arg171</scene> | ||
| - | | Y || Y || N || N || N || N || N || N || N | + | | Y || Y || N || N || N || N || N || N || N || N |
|- | |- | ||
| Stability of catalytic helix | | Stability of catalytic helix | ||
| <scene name='User:Ramiro_Barrantes/Workbench/Gstfpg/3' target="fpg">Leu4,Glu8,Arg57</scene> | | <scene name='User:Ramiro_Barrantes/Workbench/Gstfpg/3' target="fpg">Leu4,Glu8,Arg57</scene> | ||
| <scene name='User:Ramiro_Barrantes/Workbench/Econei/4' target="ecoNei">Nei?</scene> | | <scene name='User:Ramiro_Barrantes/Workbench/Econei/4' target="ecoNei">Nei?</scene> | ||
| - | | Y || Y || Y || N || N || N || N || N || N | + | | Y || Y || Y || N || N || N || N || N || N || N |
|} | |} | ||
Revision as of 15:53, 21 May 2009
Contents |
The FpgNei Protein Superfamily
Functional Units
| G. Stereothermophilus Fpg | E. Coli Nei | ||||||||||||
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| Functional Cluster | Variant 1 | Variant 2 | Fpg1 | Fpg2 | Plant | Neil1 | Neil2 | Neil3 | Proteo | Actino1 | Actino2 | MimiVirus | Support for perfectly conserved Asn168 | Y | Y | N | N | N | N | N | N | N | N | ||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Stability of catalytic helix | Y | Y | Y | N | N | N | N | N | N | N |
Functional Cluster 1: Stability of perfectly conserved Asn168
Asn168, along with two other amino acids have an effect in the orientation and kinking of the DNA. In 4 of the 9 clades (Fpg1, Fpg2 and Plants and Fungi) Asn168 is supported by Lys160, which in turn hydrogen bonds with Leu249 and Ser250. In the other clades (Actinobacteria 1 and 2, Proteacteria and all vertebrate sequences), Arg171 that comes from a different helix fulfills the same roles as Lys160. One important difference is that the Zinc Finger is shaped differently in the absence of DNA, and there is a hydrogen bond between one of the ?-sheets and the arginine. One hypothesis is that the arginine or the lysine is necessary to support the Asn168, crucial for orientation of the DNA.
