User:Wally Novak/Sandbox Miller
From Proteopedia
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| - | <Structure load='1X9N' size='350' frame='true' align='right' caption='Human DNA Ligase I' scene='Protein residues 232-919 encircling nicked DNA' /> | + | <Structure load='1X9N' size='350' frame='true' align='right' caption='Human DNA Ligase I' scene='Protein residues 232-919 encircling nicked DNA' /> |
| - | + | 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. <ref>Ellenberger, T.; Tomkinson, A.E. ''Annu. Rev. Biochem.'' '''2008''', ''77'', 13-38; Shuman, S. ''J. Biol. Chem.'' '''2009''', ''284'', 17365-17369.</ref> The ligation proceeds via a three step process uniting the 3'-OH to the 5'-phosphate with an ATP or NAD+ cofactor. <ref>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.</ref> 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. | |
| - | 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. <ref>Ellenberger, T.; Tomkinson, A.E. ''Annu. Rev. Biochem.'' '''2008''', ''77'', 13-38; Shuman, S. ''J. Biol. Chem.'' '''2009''', ''284'', 17365-17369.</ref> The ligation proceeds via a three step process uniting the 3'-OH to the 5'-phosphate with an ATP or NAD+ cofactor. <ref> | + | |
== Structural Domains == | == 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 <scene name='74/743658/Domains_for_human_dna_ligase_i/1'>scene</scene>. 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.<ref>Pascal, J.M.; O'Brien, P.J.; Tomkinson, A.E.; Ellenberger, T. ''Nature'' '''2004''', ''432'', 473-478.</ref> | DNA ligase I has four structural domains spread over a 919 residue monomeric protein. Three of the four domains are highlighted in the <scene name='74/743658/Domains_for_human_dna_ligase_i/1'>scene</scene>. 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.<ref>Pascal, J.M.; O'Brien, P.J.; Tomkinson, A.E.; Ellenberger, T. ''Nature'' '''2004''', ''432'', 473-478.</ref> | ||
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== Ligating Mechanism == | == Ligating Mechanism == | ||
Revision as of 23:57, 7 October 2016
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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.
Contents |
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
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
</StructureSection>
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.
