Fpg Nei Protein Family

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Revision as of 21:36, 18 June 2009 (edit) Ramiro Barrantes (Talk | contribs) (New page: {{STRUCTURE_3cin | PDB=1R2Y | SCENE= }} ==DNA Repair and Base Excision DNA Repair== For a video of DNA repair [http://www.youtube.com/watch?v=CcTayxEblio click here]. The picture bel...) ← Previous diff		Revision as of 15:15, 27 April 2010 (edit) (undo) Ramiro Barrantes (Talk | contribs) Next diff →
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	{{STRUCTURE_3cin | PDB=1R2Y | SCENE= }}		{{STRUCTURE_3cin | PDB=1R2Y | SCENE= }}
-	==DNA Repair and Base Excision DNA Repair==	+	The material for this page is currently under review. If you are a reviewer for the Barrantes et al. paper please go to
-	For a video of DNA repair [http://www.youtube.com/watch?v=CcTayxEblio click here]. The picture below also illustrates DNA repair:	+	[http://proteopedia.org/wiki/index.php/User:Ramiro_Barrantes/Workbench | http://proteopedia.org/wiki/index.php/User:Ramiro_Barrantes/Workbench]
-	[[Image:DNARepair.png]]	+
-	The genome of any living organisms is being continuously affected by exogenous and endogenous agents, such as ultraviolet light, ionizing radiation, different chemicals and the cell's own metabolites (such as reactive oxygen). Therefore, different systems have evolved to repair these damages. With some of these systems shared throughout all lifeforms. Therefore, the proper functioning of DNA repair is critical for survival. There are six pathways of DNA repair (reviewed in Friedberg et al), and one of the is base-excision repair. The latter's distinguishing feature is that it removes lesions as single bases, as opposed to dNMPs or short oligonucleotides like other systems. <ref>PMID: 18259689</ref>	+
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-	Base excision repair's signature enzyme are the DNA glycosylases. These enzymes work by recognizing and removing a single damaged base from DNA. They are called DNA glycosylases because they hydrolize the N-glycosidic bond of the damaged deoxynucleoside. The subsequent steps of the pathway (strand incision, gap-filling and ligation) are done by other enzymes. See below for a cartoon of the process <ref>PMID: 18259689</ref><ref>PMID:19153658</ref>:	+
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-	==Evolution and related structures==	+
-	[[Image:Picture 9.png|thumb|166px|left|Cartoon phylogenetic tree of the FpgNei protein family. Neil1 is one among several metazoan repair proteins]] Neil1 is part of the FpgNei superfamily of base excision repair proteins. And its one of 3 DNA glycosylases present in vertebrates, and in humans in particular. The evolution of this superfamily is not totally clear.	+
-	Homologous structures have been solved, including Fpg protein from Lactococcus Lactis ([[1pjj]])<ref>PMID: 16243784</ref>, Bacillus Stereothermophilus ([[1r2y]])<ref>PMID:14525999</ref>, Thermos Thermophilus ([[1ee8]])<ref>PMID:10921868</ref> and Escherichia Coli([[1k82]])<ref>PMID:11912217</ref> and Nei from Escherichia Coli ([[1k3w]])<ref>PMID:11847126</ref>. The overall structure is similar, and some of the damages include 8-oxoguanine and fapyG ([[1xc8]])<ref>PMID:15249553</ref>.	+
	==References==		==References==

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Revision as of 15:15, 27 April 2010

spinqualitylabelsall models PDB ID 1R2Y Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
3cin, resolution 1.70Å ()
Ligands:	, ,
Gene:	TM1419, TM_1419 (Thermotoga maritima MSB8)
Activity:	Inositol-3-phosphate synthase, with EC number 5.5.1.4
Structural annotation: Resources: CATH : 3Cina01, 3Cina02 InterPro : Ipr016040, Ipr013021, Ipr002587 Pfam : PF07994
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum, TOPSAN
Coordinates:	save as pdb, mmCIF, xml

The material for this page is currently under review. If you are a reviewer for the Barrantes et al. paper please go to | http://proteopedia.org/wiki/index.php/User:Ramiro_Barrantes/Workbench

References