3AAM

Crystal structure of endonuclease IV from Thermus thermophilus HB8

Summary for 3AAM

• Entry DOI: 10.2210/pdb3aam/pdb
• Related: 3AAL
• Descriptor: Endonuclease IV, MANGANESE (II) ION, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: dna repair, base excision repair, ber, tim barrel, endonuclease, hydrolase, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi
• Biological source: Thermus thermophilus
• Total number of polymer chains: 1
• Total formula weight: 29275.20

Authors

Asano, R.,Ishikawa, H.,Nakane, S.,Baba, S.,Nakagawa, N.,Kuramitsu, S.,Masui, R.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2009-11-20, release date: 2010-12-01, Last modification date: 2023-11-01)

Primary citation

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.,Sect.D, 67:149-155, 2011

PubMed Abstract: 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.

PubMed: 21358045
DOI: 10.1107/S0907444910052479

Experimental method

X-RAY DIFFRACTION (1.58 Å)