1PC6

Structural Genomics, NinB

1PC6 の概要

• エントリーDOI: 10.2210/pdb1pc6/pdb
• 分子名称: Protein ninB, BETA-MERCAPTOETHANOL (3 entities in total)
• 機能のキーワード: structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, unknown function
• 由来する生物種: Enterobacteria phage lambda
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33498.32

構造登録者

Zhang, R.,Beasley, S.,Maxwell, K.L.,Edwards, A.M.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2003-05-15, 公開日: 2004-01-20, 最終更新日: 2025-03-26)

主引用文献

Maxwell, K.L.,Reed, P.,Zhang, R.,Beasley, S.,Walmsley, A.R.,Curtis, F.A.,Joachimiak, A.,Edwards, A.M.,Sharples, G.J.
Functional similarities between phage lambda Orf and Escherichia coli RecFOR in initiation of genetic exchange
Proc.Natl.Acad.Sci.USA, 102:11260-11265, 2005

PubMed Abstract: Genetic recombination in bacteriophage lambda relies on DNA end processing by Exo to expose 3'-tailed strands for annealing and exchange by beta protein. Phage lambda encodes an additional recombinase, Orf, which participates in the early stages of recombination by supplying a function equivalent to the Escherichia coli RecFOR complex. These host enzymes assist loading of the RecA strand exchange protein onto ssDNA coated with ssDNA-binding protein. In this study, we purified the Orf protein, analyzed its biochemical properties, and determined its crystal structure at 2.5 angstroms. The homodimeric Orf protein is arranged as a toroid with a shallow U-shaped cleft, lined with basic residues, running perpendicular to the central cavity. Orf binds DNA, favoring single-stranded over duplex and with no obvious preference for gapped, 3'-tailed, or 5'-tailed substrates. An interaction between Orf and ssDNA-binding protein was indicated by far Western analysis. The functional similarities between Orf and RecFOR are discussed in relation to the early steps of recombinational exchange and the interplay between phage and bacterial recombinases.

PubMed: 16076958
DOI: 10.1073/pnas.0503399102

実験手法

X-RAY DIFFRACTION (2.51 Å)