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	=== Functional Cluster 1: Stability of perfectly conserved Asn168 ===		=== Functional Cluster 1: Stability of perfectly conserved Asn168 ===
-	[[Image:F1WebLogo.jpg]] 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.	+	[[Image:F1WebLogo.jpg|thumb|166px|left|WebLogo for the first functional unit, note the covariation between lysine nad arginine]] 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 beta-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 ==		== Evolution ==
	== References ==		== References ==

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Revision as of 16:06, 21 May 2009

Contents 1 The FpgNei Protein Superfamily 1.1 Functional Units 1.1.1 Functional Cluster 1: Stability of perfectly conserved Asn168 1.2 Evolution 1.3 References

The FpgNei Protein Superfamily

Functional Units

G. Stereothermophilus Fpg	E. Coli Nei
spinqualitylabelsall models Bacterial Fpg Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image	spinqualitylabelsall models E. coli Nei Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 beta-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