User:Wally Novak/Sandbox Miller
From Proteopedia
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DNA ligases are a group of proteins responsible for the joining DNA fragments which arise from various cellular events: ligating Okazaki fragments from replication, various repair mechanisms, and recombination. [1] The ligation proceeds via a three step process uniting the 3'-OH to the 5'-phosphate with an ATP or NAD+ cofactor. [2] DNA ligase I is a member of this family expressed throughout eukaryotes. Included is a summary of its functionality covering the conserved structural domains, ligating mechanism, and involvement in replication as well as DNA repair mechanisms.
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Structural Domains
DNA ligase I has four structural domains spread over a 919 residue monomeric protein. Three of the four domains are highlighted in the . The DNA-binding domain (DBD) is in red; the adenylation domain (AdD), green; the OB-fold domain (OBD), yellow; and the DNA, grey. The first 232 residues containing domains that interact with other regulative proteins were excluded from the source structure that Ellenberger and colleagues studied.[3]
Ligating Mechanism
Okazaki Fragments and Replication
DNA Repair
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References
- ↑ Ellenberger, T.; Tomkinson, A.E. Annu. Rev. Biochem. 2008, 77, 13-38; Shuman, S. J. Biol. Chem. 2009, 284, 17365-17369.
- ↑ Ellenberger, T.; Tomkinson, A.E. Annu. Rev. Biochem. 2008, 77, 13-38; Shuman, S. J. Biol. Chem. 2009, 284, 17365-17369; Tomkinson, A.E.; Vijayakumar, S.; Pascal, J.M.; Ellenberger, T. Chem. Rev. 2006, 106, 687-669.
- ↑ Pascal, J.M.; O'Brien, P.J.; Tomkinson, A.E.; Ellenberger, T. Nature 2004, 432, 473-478.
[1] to the rescue.
