1T94

Crystal structure of the catalytic core of human DNA polymerase kappa

1T94 の概要

• エントリーDOI: 10.2210/pdb1t94/pdb
• 分子名称: polymerase (DNA directed) kappa (2 entities in total)
• 機能のキーワード: replication; dna repair; y-family dna polymerase; translesion dna synthesis; lesion bypass, replication
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus : Q9UBT6
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 104805.58

構造登録者

Uljon, S.N.,Johnson, R.E.,Edwards, T.A.,Prakash, S.,Prakash, L.,Aggarwal, A.K. (登録日: 2004-05-14, 公開日: 2004-08-31, 最終更新日: 2024-02-14)

主引用文献

Uljon, S.N.,Johnson, R.E.,Edwards, T.A.,Prakash, S.,Prakash, L.,Aggarwal, A.K.
Crystal structure of the catalytic core of human DNA polymerase kappa.
STRUCTURE, 12:1395-1404, 2004

PubMed Abstract: We present the crystal structure of the catalytic core of human DNA polymerase kappa (hPolkappa), the first structure of a human Y-family polymerase. hPolkappa is implicated in the proficient extension of mispaired primer termini on undamaged DNAs, and in the extension step of lesion bypass. The structure reveals a stubby "fingers" subdomain, which despite its small size appears to be tightly restrained with respect to a putative templating base. The structure also reveals a novel "thumb" subdomain that provides a basis for the importance of the N-terminal extension unique to hPolkappa. And, most surprisingly, the structure reveals the polymerase-associated domain (PAD) juxtaposed on the dorsal side of the "palm" subdomain, as opposed to the fingers subdomain. Together, these properties suggest that the hPolkappa active site is constrained at the site of the templating base and incoming nucleotide, but the polymerase is less constrained following translocation of the lesion.

PubMed: 15296733
DOI: 10.1016/j.str.2004.05.011

実験手法

X-RAY DIFFRACTION (2.4 Å)