2FLN

binary complex of catalytic core of human DNA polymerase iota with DNA (template A)

2FLN の概要

• エントリーDOI: 10.2210/pdb2fln/pdb
• 関連するPDBエントリー: 1T3N 2ALZ 2FLL 2FLP
• 分子名称: DNA template strand, DNA primer strand, DNA polymerase iota, ... (4 entities in total)
• 機能のキーワード: dna polymerase, lesion bypass, binary complex, template a, replication-dna complex, replication/dna
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q9UNA4
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 52458.94

構造登録者

Nair, D.T.,Johnson, R.E.,Prakash, L.,Prakash, S.,Aggarwal, A.K. (登録日: 2006-01-06, 公開日: 2006-12-05, 最終更新日: 2023-08-30)

主引用文献

Nair, D.T.,Johnson, R.E.,Prakash, L.,Prakash, S.,Aggarwal, A.K.
An incoming nucleotide imposes an anti to syn conformational change on the templating purine in the human DNA polymerase-iota active site.
Structure, 14:749-755, 2006

PubMed Abstract: Substrate-induced conformational change of the protein is the linchpin of enzymatic reactions. Replicative DNA polymerases, for example, convert from an open to a closed conformation in response to dNTP binding. Human DNA polymerase-iota (hPoliota), a member of the Y family of DNA polymerases, differs strikingly from other polymerases in its much higher proficiency and fidelity for nucleotide incorporation opposite template purines than opposite template pyrimidines. We present here a crystallographic analysis of hPoliota binary complexes, which together with the ternary complexes show that, contrary to replicative DNA polymerases, the DNA, and not the polymerase, undergoes the primary substrate-induced conformational change. The incoming dNTP "pushes" templates A and G from the anti to the syn conformation dictated by a rigid hPoliota active site. Together, the structures posit a mechanism for template selection wherein dNTP binding induces a conformational switch in template purines for productive Hoogsteen base pairing.

PubMed: 16615915
DOI: 10.1016/j.str.2006.01.010

実験手法

X-RAY DIFFRACTION (2.5 Å)