2X7W

Crystal structure of Thermotoga maritima endonuclease IV in the presence of cadmium and zinc

Summary for 2X7W

• Entry DOI: 10.2210/pdb2x7w/pdb
• Related: 2X7V
• Descriptor: PROBABLE ENDONUCLEASE 4, ZINC ION, CADMIUM ION, ... (5 entities in total)
• Functional Keywords: nuclease, hydrolase, dna repair, apurinic-apyrimidinic (ap) metal-binding
• Biological source: THERMOTOGA MARITIMA MSB8
• Total number of polymer chains: 1
• Total formula weight: 32936.32

Authors

Tomanicek, S.J.,Hughes, R.C.,Ng, J.D.,Coates, L. (deposition date: 2010-03-03, release date: 2010-09-08, Last modification date: 2023-12-20)

Primary citation

Tomanicek, S.J.,Hughes, R.C.,Ng, J.D.,Coates, L.
Structure of the Endonuclease Iv Homologue from Thermotoga Maritima in the Presence of Active-Site Divalent Metal Ions
Acta Crystallogr.,Sect.F, 66:1003-, 2010

PubMed Abstract: The most frequent lesion in DNA is at apurinic/apyrimidinic (AP) sites resulting from DNA-base losses. These AP-site lesions can stall DNA replication and lead to genome instability if left unrepaired. The AP endonucleases are an important class of enzymes that are involved in the repair of AP-site intermediates during damage-general DNA base-excision repair pathways. These enzymes hydrolytically cleave the 5'-phosphodiester bond at an AP site to generate a free 3'-hydroxyl group and a 5'-terminal sugar phosphate using their AP nuclease activity. Specifically, Thermotoga maritima endonuclease IV is a member of the second conserved AP endonuclease family that includes Escherichia coli endonuclease IV, which is the archetype of the AP endonuclease superfamily. In order to more fully characterize the AP endonuclease family of enzymes, two X-ray crystal structures of the T. maritima endonuclease IV homologue were determined in the presence of divalent metal ions bound in the active-site region. These structures of the T. maritima endonuclease IV homologue further revealed the use of the TIM-barrel fold and the trinuclear metal binding site as important highly conserved structural elements that are involved in DNA-binding and AP-site repair processes in the AP endonuclease superfamily.

PubMed: 20823514
DOI: 10.1107/S1744309110028575

Experimental method

X-RAY DIFFRACTION (2.36 Å)