3aal

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Crystal Structure of endonuclease IV from Geobacillus kaustophilusCrystal Structure of endonuclease IV from Geobacillus kaustophilus

Structural highlights

3aal is a 1 chain structure with sequence from Geobacillus kaustophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:GK2474 (Geobacillus kaustophilus)
Activity:Deoxyribonuclease IV (phage-T(4)-induced), with EC number 3.1.21.2
Resources:FirstGlance, OCA, RCSB, PDBsum

Publication Abstract from PubMed

Endonuclease IV (EndoIV) is an endonuclease that acts at apurinic/apyrimidinic (AP) sites and is classified as either long-type or short-type. The crystal structures of representative types of EndoIV from Geobacillus kaustophilus and Thermus thermophilus HB8 were determined using X-ray crystallography. G. kaustophilus EndoIV (the long type) had a higher affinity for double-stranded DNA containing an AP-site analogue than T. thermophilus EndoIV (the short type). Structural analysis of the two different EndoIVs suggested that a C-terminal DNA-recognition loop that is only present in the long type contributes to its high affinity for AP sites. A mutation analysis showed that Lys267 in the C-terminal DNA-recognition loop plays an important role in DNA binding.

An additional C-terminal loop in endonuclease IV, an apurinic/apyrimidinic endonuclease, controls binding affinity to DNA.,Asano R, Ishikawa H, Nakane S, Nakagawa N, Kuramitsu S, Masui R Acta Crystallogr D Biol Crystallogr. 2011 Mar;67(Pt 3):149-55. Epub 2011, Feb 15. PMID:21358045[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Asano R, Ishikawa H, Nakane S, Nakagawa N, Kuramitsu S, Masui R. An additional C-terminal loop in endonuclease IV, an apurinic/apyrimidinic endonuclease, controls binding affinity to DNA. Acta Crystallogr D Biol Crystallogr. 2011 Mar;67(Pt 3):149-55. Epub 2011, Feb 15. PMID:21358045 doi:10.1107/S0907444910052479

3aal, resolution 1.60Å

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