3QZ7

T-3 ternary complex of Dpo4

3QZ7 の概要

• エントリーDOI: 10.2210/pdb3qz7/pdb
• 関連するPDBエントリー: 3QZ8
• 分子名称: DNA polymerase IV, 5'-D(*GP*GP*CP*AP*CP*TP*GP*AP*TP*CP*GP*GP*G)-3', 5'-D(*TP*TP*AP*CP*GP*CP*CP*TP*CP*GP*AP*TP*CP*AP*GP*TP*GP*CP*C)-3', ... (6 entities in total)
• 機能のキーワード: lesion bypass, single-base deletion, -1 frameshift, replication-dna complex, transferase-dna complex, transferase/dna
• 由来する生物種: Sulfolobus solfataricus
• 細胞内の位置: Cytoplasm (Probable): Q97W02
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 51577.59

構造登録者

Pata, J.D.,Wu, Y.,Wilson, R.C. (登録日: 2011-03-04, 公開日: 2011-04-06, 最終更新日: 2023-09-13)

主引用文献

Wu, Y.,Wilson, R.C.,Pata, J.D.
The y-family DNA polymerase dpo4 uses a template slippage mechanism to create single-base deletions.
J.Bacteriol., 193:2630-2636, 2011

PubMed Abstract: The Y-family polymerases help cells tolerate DNA damage by performing translesion synthesis, yet they also can be highly error prone. One distinctive feature of the DinB class of Y-family polymerases is that they make single-base deletion errors at high frequencies in repetitive sequences, especially those that contain two or more identical pyrimidines with a 5' flanking guanosine. Intriguingly, different deletion mechanisms have been proposed, even for two archaeal DinB polymerases that share 54% sequence identity and originate from two strains of Sulfolobus. To reconcile these apparent differences, we have characterized Dpo4 from Sulfolobus solfataricus using the same biochemical and crystallographic approaches that we have used previously to characterize Dbh from Sulfolobus acidocaldarius. In contrast to previous suggestions that Dpo4 uses a deoxynucleoside triphosphate (dNTP)-stabilized misalignment mechanism when creating single-base deletions, we find that Dpo4 predominantly uses a template slippage deletion mechanism when replicating repetitive DNA sequences, as was previously shown for Dbh. Dpo4 stabilizes the skipped template base in an extrahelical conformation between the polymerase and the little-finger domains of the enzyme. This contrasts with Dbh, in which the extrahelical base is stabilized against the surface of the little-finger domain alone. Thus, despite sharing a common deletion mechanism, these closely related polymerases use different contacts with the substrate to accomplish the same result.

PubMed: 21421759
DOI: 10.1128/JB.00012-11

実験手法

X-RAY DIFFRACTION (1.998 Å)