4F4Z

Y-family DNA polymerase chimera Dpo4-Dpo4-Dbh

4F4Z の概要

• エントリーDOI: 10.2210/pdb4f4z/pdb
• 関連するPDBエントリー: 4F4W 4F4X 4F4Y 4F50
• 分子名称: DNA polymerase IV, DNA (5'-D(*AP*GP*GP*GP*GP*GP*AP*AP*GP*CP*CP*G)-3'), DNA (5'-D(*TP*TP*CP*CP*GP*CP*CP*CP*GP*GP*CP*TP*TP*CP*CP*CP*CP*CP*T)-3'), ... (5 entities in total)
• 機能のキーワード: y-family polymerase, transferase-dna complex, transferase/dna
• 由来する生物種: Sulfolobus solfataricus; 詳細
• 細胞内の位置: Cytoplasm : Q4JB80
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 101306.50

構造登録者

Pata, J.D.,Wilson, R.C. (登録日: 2012-05-11, 公開日: 2013-01-02, 最終更新日: 2024-02-28)

主引用文献

Wilson, R.C.,Jackson, M.A.,Pata, J.D.
Y-family polymerase conformation is a major determinant of fidelity and translesion specificity.
Structure, 21:20-31, 2013

PubMed Abstract: Y-family polymerases help cells tolerate DNA damage by performing translesion synthesis opposite damaged DNA bases, yet they also have a high intrinsic error rate. We constructed chimeras of two closely related Y-family polymerases that display distinctly different activity profiles and found that the polypeptide linker that tethers the catalytic polymerase domain to the C-terminal DNA-binding domain is a major determinant of overall polymerase activity, nucleotide incorporation fidelity, and abasic site-bypass ability. Exchanging just 3 out of the 15 linker residues is sufficient to interconvert the polymerase activities tested. Crystal structures of four chimeras show that the conformation of the protein correlates with the identity of the interdomain linker sequence. Thus, residues that are more than 15 Å away from the active site are able to influence many aspects of polymerase activity by altering the relative orientations of the catalytic and DNA-binding domains.

PubMed: 23245850
DOI: 10.1016/j.str.2012.11.005

実験手法

X-RAY DIFFRACTION (2.305 Å)