DNA ligase
From Proteopedia
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| - | '''DNA ligase''' (LigD) is an enzyme which repairs single-stranded breaks in a double-stranded DNA. LigD is activated , in a species-dependent manner, by hydrolysis of ATP or NAD+. Mammalian LigD I ligates the nascent DNA of the lagging strand; LigD III complexes with XRCC1 in the process of nucleotide excision repair; LigD IV complexes with XRCC4 and catalyzes the last step in the non-homologous DNA end joining. | + | '''DNA ligase''' (LigD) is an enzyme which repairs single-stranded breaks in a double-stranded DNA. LigD is activated , in a species-dependent manner, by hydrolysis of ATP or NAD+. Mammalian LigD I ligates the nascent DNA of the lagging strand; LigD III complexes with XRCC1 in the process of nucleotide excision repair; LigD IV complexes with XRCC4 and catalyzes the last step in the non-homologous DNA end joining.LigD contains several domains: adenylation domain; DNA-binding domain and the ca. 100 amino acid long BRCT motif. |
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== 3D Structures of DNA ligase == | == 3D Structures of DNA ligase == | ||
| - | ''Update | + | ''Update January 2013'' |
===ATP-dependent LigD=== | ===ATP-dependent LigD=== | ||
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[[2cfm]] - LigD + AMP – ''Pyrococcus furiosus''<br /> | [[2cfm]] - LigD + AMP – ''Pyrococcus furiosus''<br /> | ||
[[2fao]] - PaLigD polymerase domain – ''Pseudomonas aeruginosa''<br /> | [[2fao]] - PaLigD polymerase domain – ''Pseudomonas aeruginosa''<br /> | ||
| - | [[2faq]], [[ 2far]] - PaLigD polymerase domain + ATP + Mn<br /> | + | [[2faq]], [[2far]] - PaLigD polymerase domain + ATP + Mn<br /> |
[[1a0i]] – LigD + ATP – Bacteriophage T7<br /> | [[1a0i]] – LigD + ATP – Bacteriophage T7<br /> | ||
[[4eq5]] – LigD + AMP – ''Thermococcus sibiricus'' | [[4eq5]] – LigD + AMP – ''Thermococcus sibiricus'' | ||
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===NAD+-dependent LigD=== | ===NAD+-dependent LigD=== | ||
| - | [[3jsl]], [[ 3jsn]] - LigD adenylation domain – ''Staphylococcus aureus''<br /> | + | [[3jsl]], [[3jsn]] - LigD adenylation domain – ''Staphylococcus aureus''<br /> |
| - | [[3ba8]], [[ 3ba9]], [[ 3baa]], [[ 3bab]], [[ 3bac]] - EfLigD adenylation domain + inhibitor – ''Enterococcus faecalis''<br /> | + | [[3ba8]], [[3ba9]], [[3baa]], [[3bab]], [[3bac]] - EfLigD adenylation domain + inhibitor – ''Enterococcus faecalis''<br /> |
| - | [[1ta8]], [[ 1tae]] - EfLigD adenylation domain<br /> | + | [[1ta8]], [[1tae]] - EfLigD adenylation domain<br /> |
| - | [[1zau]] - | + | [[1zau]] - MtLigD adenylation domain – ''Mycobacterium tuberculosis''<br /> |
| - | [[1v9p]], [[ 1dgs]] – LigD – ''Thermos filiformis''<br /> | + | [[3sgi]] – MtLigD (mutant) + AMP<br /> |
| - | [[1b04]] – LigD adenylation domain (mutant) – ''Geobacillus stearothermophilus'' | + | [[1v9p]], [[1dgs]] – LigD – ''Thermos filiformis''<br /> |
| + | [[1b04]] – LigD adenylation domain (mutant) – ''Geobacillus stearothermophilus''<br /> | ||
| + | [[4glw]] – LigD A + NMN + inhibitor – ''Streptococcus pneumoniae'' | ||
===LigD=== | ===LigD=== | ||
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[[3ii6]], [[ 1ik9]] – hLigD IV C-terminal BRCT domains + DNA repair protein XRCC4<br /> | [[3ii6]], [[ 1ik9]] – hLigD IV C-terminal BRCT domains + DNA repair protein XRCC4<br /> | ||
[[2e2w]] - hLigD IV BRCT domain - NMR<br /> | [[2e2w]] - hLigD IV BRCT domain - NMR<br /> | ||
| - | [[1z56]] – LigD IV + ligase interacting factor 1 - yeast | + | [[1z56]] – LigD IV + ligase interacting factor 1 - yeast<br /> |
| + | [[3vnn]] - hLigD IV adenylation domain<br /> | ||
| + | [[4hto]] - hLigD IV DNA-binding domain<br /> | ||
| + | [[4htp]] - hLigD IV DNA-binding domain + artemis protein peptide | ||
</StructureSection> | </StructureSection> | ||
Revision as of 12:23, 30 January 2013
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REFERENCES
Elevated expression of DNA ligase I in human cancers., Sun DY, Urrabaz R, Nguyen M, Marty J, Stringer S, Cruz E, Medina-Gundrum L, Weitman S., Clinical Cancer Research. 2001; 7(12):4143-4148.
Replication failure, genome instability, and increased cancer susceptibility in mice with a point mutation in the DNA ligase I gene., Harrison C, Ketchen AM, Redhead NJ, O'Sullivan MJ, Melton DW., Cancer Research. 2002; 62(14):4065-4074.
- Created with the participation of Audrey Kuan.
