2NS6

Crystal Structure of the Minimal Relaxase Domain of MobA from Plasmid R1162

2NS6 の概要

• エントリーDOI: 10.2210/pdb2ns6/pdb
• 分子名称: Mobilization protein A, MANGANESE (II) ION (3 entities in total)
• 機能のキーワード: nickase, 5-strand antiparallel beta sheet, metalloenzyme, hydrolase
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20979.01

構造登録者

Monzingo, A.F.,Ozburn, A.,Xia, S.,Meyer, R.J.,Robertus, J.D. (登録日: 2006-11-03, 公開日: 2007-02-06, 最終更新日: 2023-12-27)

主引用文献

Monzingo, A.F.,Ozburn, A.,Xia, S.,Meyer, R.J.,Robertus, J.D.
The Structure of the Minimal Relaxase Domain of MobA at 2.1 A Resolution.
J.Mol.Biol., 366:165-178, 2007

PubMed Abstract: The plasmid R1162 encodes proteins that enable its conjugative mobilization between bacterial cells. It can transfer between many different species and is one of the most promiscuous of the mobilizable plasmids. The plasmid-encoded protein MobA, which has both nicking and priming activities on single-stranded DNA, is essential for mobilization. The nicking, or relaxase, activity has been localized to the 186 residue N-terminal domain, called minMobA. We present here the 2.1 A X-ray structure of minMobA. The fold is similar to that seen for two other relaxases, TraI and TrwC. The similarity in fold, and action, suggests these enzymes are evolutionary homologs, despite the lack of any significant amino acid similarity. MinMobA has a well- defined target DNA called oriT. The active site metal is observed near Tyr25, which is known to form a phosphotyrosine adduct with the substrate. A model of the oriT substrate complexed with minMobA has been made, based on observed substrate binding to TrwC and TraI. The model is consistent with observations of substrate base specificity, and provides a rationalization for elements of the likely enzyme mechanism.

PubMed: 17157875
DOI: 10.1016/j.jmb.2006.11.031

実験手法

X-RAY DIFFRACTION (2.1 Å)