3FTO
Crystal structure of OppA in a open conformation
Summary for 3FTO
| Entry DOI | 10.2210/pdb3fto/pdb |
| Related | 3DRF 3DRG 3DRH 3DRI 3DRJ 3DRK |
| Descriptor | Oligopeptide-binding protein oppA (2 entities in total) |
| Functional Keywords | oligo-peptide binding, voluminous binding cavity, venus fly-trap, peptide binding protein |
| Biological source | Lactococcus lactis subsp. cremoris |
| Total number of polymer chains | 1 |
| Total formula weight | 65801.32 |
| Authors | Berntsson, R.P.-A.,Oktaviani, N.A.,Fusetti, F.,Thunnissen, A.-M.W.H.,Poolman, B.,Slotboom, D.-J. (deposition date: 2009-01-13, release date: 2009-03-31, Last modification date: 2024-11-20) |
| Primary citation | 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 Cited by 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: 19388077DOI: 10.1002/pro.97 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.38 Å) |
Structure validation
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