3FTO

Crystal structure of OppA in a open conformation

3FTO の概要

• エントリーDOI: 10.2210/pdb3fto/pdb
• 関連するPDBエントリー: 3DRF 3DRG 3DRH 3DRI 3DRJ 3DRK
• 分子名称: Oligopeptide-binding protein oppA (2 entities in total)
• 機能のキーワード: oligo-peptide binding, voluminous binding cavity, venus fly-trap, peptide binding protein
• 由来する生物種: Lactococcus lactis subsp. cremoris
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 65801.32

構造登録者

Berntsson, R.P.-A.,Oktaviani, N.A.,Fusetti, F.,Thunnissen, A.-M.W.H.,Poolman, B.,Slotboom, D.-J. (登録日: 2009-01-13, 公開日: 2009-03-31, 最終更新日: 2017-11-01)

主引用文献

Berntsson, R.P.,Alia Oktaviani, N.,Fusetti, F.,Thunnissen, A.M.,Poolman, B.,Slotboom, D.J.
Selenomethionine incorporation in proteins expressed in Lactococcus lactis.
Protein Sci., 18:1121-1127, 2009

PubMed Abstract: Lactococcus lactis is a promising host for (membrane) protein overproduction. Here, we describe a protocol for incorporation of selenomethionine (SeMet) into proteins expressed in L. lactis. Incorporation efficiencies of SeMet in the membrane protein complex OpuA (an ABC transporter) and the soluble protein OppA, both from L. lactis, were monitored by mass spectrometry. Both proteins incorporated SeMet with high efficiencies (>90%), which greatly extends the usefulness of the expression host L. lactis for X-ray crystallography purposes. The crystal structure of ligand-free OppA was determined at 2.4 A resolution by a semiautomatic approach using selenium single-wavelength anomalous diffraction phasing.

PubMed: 19388077
DOI: 10.1002/pro.97

実験手法

X-RAY DIFFRACTION (2.38 Å)