DNA ligase

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== Function ==
== Function ==
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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+.<br />
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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+. See also [[ATP-dependent DNA ligase from bacteriophage T7]].<br />
* Mammalian '''LigD I''' ligates the nascent DNA of the lagging strand.<br />
* Mammalian '''LigD I''' ligates the nascent DNA of the lagging strand.<br />
* '''LigD III''' complexes with XRCC1 in the process of nucleotide excision repair.<br />
* '''LigD III''' complexes with XRCC1 in the process of nucleotide excision repair.<br />
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Human LigD IV contains several domains: DNA-binding domain (residues 1-240); adenylation domain (residues 268-405) and the ca. 100 amino acid long BRCT motifs (residues 654-911). In the ATP-dependent LigD the ATP binds between 2 symmetry related LigD molecules.
Human LigD IV contains several domains: DNA-binding domain (residues 1-240); adenylation domain (residues 268-405) and the ca. 100 amino acid long BRCT motifs (residues 654-911). In the ATP-dependent LigD the ATP binds between 2 symmetry related LigD molecules.
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*<scene name='44/443730/Cv/3'>ATP binding site</scene> in ATP-dependent DNA ligase from ''S. solfataricus'' ([[2hix]]). <ref>PMID:17052461</ref>
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*<scene name='44/443730/Cv/4'>ATP binding site</scene> in ATP-dependent DNA ligase from ''S. solfataricus'' ([[2hix]]). <ref>PMID:17052461</ref>
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</StructureSection>
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== 3D Structures of DNA ligase ==
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== 3D Structures of DNA ligase ==
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[[DNA ligase 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*ATP-dependent LigD
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**[[3p4h]], [[3ta5]], [[3ta7]] – LigD N-terminal – ''Candidatus korarchaeum cryptofilum''<br />
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**[[3gde]] – LigD – ''Archaeoglobus fulgidus''<br />
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**[[2hiv]] – SsLigD – ''Sulfolobus solfataricus''<br />
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**[[2hix]] - SsLigD + ATP<br />
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**[[2cfm]] - LigD + AMP – ''Pyrococcus furiosus''<br />
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**[[2fao]] - PaLigD polymerase domain – ''Pseudomonas aeruginosa''<br />
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**[[2faq]], [[2far]] - PaLigD polymerase domain + ATP + Mn<br />
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**[[1a0i]] – LigD + ATP – Bacteriophage T7<br />
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**[[4eq5]] – LigD + AMP – ''Thermococcus sibiricus''
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*NAD+-dependent LigD
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**[[3jsl]], [[3jsn]] - LigD adenylation domain – ''Staphylococcus aureus''<br />
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**[[3ba8]], [[3ba9]], [[3baa]], [[3bab]], [[3bac]], [[4eeq]], [[4efb]], [[4efe]], [[4lh6]], [[4lh7]] - EfLigD adenylation domain + NMN + inhibitor – ''Enterococcus faecalis''<br />
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**[[1ta8]], [[1tae]] - EfLigD adenylation domain<br />
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**[[1zau]] - MtLigD adenylation domain – ''Mycobacterium tuberculosis''<br />
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**[[3sgi]] – MtLigD (mutant) + AMP<br />
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**[[1v9p]], [[1dgs]] – LigD – ''Thermos filiformis''<br />
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**[[1b04]] – LigD adenylation domain (mutant) – ''Geobacillus stearothermophilus''<br />
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**[[4glw]] – LigD A + NMN + inhibitor – ''Streptococcus pneumoniae''<br />
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**[[4glx]] – LigD + DNA + inhibitor - ''Escherichia coli''<br />
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*LigD
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**[[2q2t]] – CvLigD + DNA + AMP + CMP – Chlorella virus<br />
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**[[2q2u]], [[ 1p8l]], [[ 1fvi]] - CvLigD + DNA + mononucleotide<br />
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**[[2owo]] – LigD + DNA + AMP + CMP – ''Escherichia coli''<br />
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**[[3qwu]] – LigD – ''Aquifex aeolicus''<br />
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**[[3pn1]] – HiLigD adenylation domain + inhibitor – ''Haemophilus influenzae''<br />
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**[[3uq8]] - HiLigD adenylation domain + NAD<br />
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**[[1l7b]] – LigD BRCT domain – ''Thermos thermophilus'' - NMR<br />
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**[[3rr5]] – LigD - ''Thermococcus''
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*Mammalian LigD I
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**[[1x9n]] – hLigD I + DNA + AMP + CMP – human<br />
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**[[2od8]] – LigD I residues 32-53 + PCNA
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*Mammalian LigD III
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**[[3l2p]] – hLigD III residues 257-833 + DNA<br />
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**[[1uw0]] - hLigD III zinc-finger domain residues 1-117 – NMR<br />
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**[[1imo]], [[1in1]] - hLigD III BRCTdomain – NMR<br />
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**[[3pc7]] - hLigD III BRCTdomain<br />
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**[[3pc8]] - hLigD III BRCTdomain (mutant) + XRCC1<br />
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**[[3qvg]] - hLigD III BRCTdomain + XRCC1
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*Mammalian LigD IV
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**[[3ii6]], [[ 1ik9]] – hLigD IV C-terminal BRCT domains + DNA repair protein XRCC4<br />
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**[[3w5o]] - hLigD IV <br />
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**[[2e2w]] - hLigD IV BRCT domain - NMR<br />
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**[[1z56]] – LigD IV + ligase interacting factor 1 - yeast<br />
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**[[3vnn]] - hLigD IV adenylation domain<br />
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**[[4hto]] - hLigD IV DNA-binding domain<br />
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**[[4htp]] - hLigD IV DNA-binding domain + artemis protein peptide<br />
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**[[3w1b]], [[3w1g]] - hLigD IV adenylation and DNA-binding domains + artemis protein peptide<br />
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}}
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== References ==
== References ==

Current revision

ATP-dependent DNA ligase complexed with ATP 2hix

Drag the structure with the mouse to rotate

References

  1. Pascal JM, Tsodikov OV, Hura GL, Song W, Cotner EA, Classen S, Tomkinson AE, Tainer JA, Ellenberger T. A flexible interface between DNA ligase and PCNA supports conformational switching and efficient ligation of DNA. Mol Cell. 2006 Oct 20;24(2):279-91. PMID:17052461 doi:10.1016/j.molcel.2006.08.015

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.

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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