4EQ5

DNA ligase from the archaeon Thermococcus sibiricus

Summary for 4EQ5

• Entry DOI: 10.2210/pdb4eq5/pdb
• Related: 2CFM 2HIV 3GDE 3RR5
• Descriptor: DNA ligase, ADENOSINE MONOPHOSPHATE (3 entities in total)
• Functional Keywords: dna-binding domain, adenylation domain, atp-dependent thermostable dna ligase, archaeon thermococcus sibiricus, ligase
• Biological source: Thermococcus sibiricus
• Total number of polymer chains: 1
• Total formula weight: 65162.98

Authors

Petrova, T.,Bezsudnova, E.Y.,Dorokhov, B.D.,Slutskaya, E.S.,Polyakov, K.M.,Dorovatovskiy, P.V.,Ravin, N.V.,Skryabin, K.G.,Kovalchuk, M.V.,Popov, V.O. (deposition date: 2012-04-18, release date: 2012-05-09, Last modification date: 2023-09-13)

Primary citation

Petrova, T.E.,Bezsudnova, E.Y.,Dorokhov, B.D.,Slutskaya, E.S.,Polyakov, K.M.,Dorovatovskiy, P.V.,Ravin, N.V.,Skryabin, K.G.,Kovalchuk, M.V.,Popov, V.O.
Expression, purification, crystallization and preliminary crystallographic analysis of a thermostable DNA ligase from the archaeon Thermococcus sibiricus.
Acta Crystallogr.,Sect.F, 68:163-165, 2012

PubMed Abstract: DNA ligases join single-strand breaks in double-stranded DNA by catalyzing the formation of a phosphodiester bond between adjacent 5'-phosphate and 3'-hydroxyl termini. Their function is essential to maintain the integrity of the genome in DNA replication, recombination and repair. A recombinant ATP-dependent DNA ligase from the hyperthermophilic anaerobic archaeon Thermococcus sibiricus was expressed in Escherichia coli and purified. Crystals were grown by vapour diffusion using the hanging-drop method with 17%(w/v) PEG 4000 and 8.5%(v/v) 2-propanol as precipitants. A diffraction experiment was performed with a single crystal, which diffracted X-rays to 3.0 Å resolution. The crystal belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 58.590, b = 87.540, c = 126.300 Å.

PubMed: 22297989
DOI: 10.1107/S1744309111050913

Experimental method

X-RAY DIFFRACTION (2.85 Å)