User:Ramiro Barrantes/FpgNeiRepair

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(Functional Units)
(Functional Units)
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! Functional Cluster !! Variant 1 !! Variant 2 !! Fpg1 !! Fpg2 !! Plant !! Neil1 !! Neil2 !! Neil3 !! Proteo !! Actino1 !! Actino2 !! MimiVirus
! Functional Cluster !! Variant 1 !! Variant 2 !! Fpg1 !! Fpg2 !! Plant !! Neil1 !! Neil2 !! Neil3 !! Proteo !! Actino1 !! Actino2 !! MimiVirus
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| Support for perfectly conserved Asn168
| Support for perfectly conserved Asn168
| <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>

Revision as of 15:54, 21 May 2009

Contents

The FpgNei Protein Superfamily

Functional Units

G. Stereothermophilus Fpg E. Coli Nei

Bacterial Fpg

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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.

Evolution

References

Proteopedia Page Contributors and Editors (what is this?)

Ramiro Barrantes, Jaime Prilusky

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