The crystal structure of a microcomparments protein from Desulfitobacterium hafniense DCB
Midwest Center for Structural Genomics (MCSG)
Structure of a PduT homolog from a novel bacterial microcompartment
A(MSE)ESIGLVEVNSIARGIEAADA(MSE)LKAAQVDLLEAKPVCPGKYIVLICGDVAAVQSSVTAGKT(MSE)AAHSV LDDFILPNVHPQVLTAISAATPLTLIKALGIIETFSIASLIVAADTAAKTGQVDLVEIRIG(MSE)GIGGKSFVTLTGDV ASVESSVAAGV(MSE)LASERG(MSE)LVDKVVIPSPHDHLKRCLC
AMESIGLVEVNSIARGIEAADAMLKAAQVDLLEAKPVCPGKYIVLICGDVAAVQSSVTAGKTMAAHSVLDDFILPNVHPQ VLTAISAATPLTLIKALGIIETFSIASLIVAADTAAKTGQVDLVEIRIGMGIGGKSFVTLTGDVASVESSVAAGVMLASE RGMLVDKVVIPSPHDHLKRCLC
30% (w/v) PEG400, 0.2M magnesium chloride, 0.1M HEPES at pH7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K
HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Size exclusion chromatography confirms the presence of trimers. Two copies of trimer can potentially stack together and form a hexamer, as found in crystal lattice.
Structural Genomics, PSI-2, Protein Structure Initiative, Midwest Center for Structural Genomics, MCSG, BMC domain, STRUCTURAL PROTEIN
MESIGLVEVNSIARGIEAADAMLKAAQVDLLEAKPVCPGKYIVLICGDVAAVQSSVTAGKTMAAHSVLDDFILPNVHPQV LTAISAATPLTLIKALGIIETFSIASLIVAADTAAKTGQVDLVEIRIGMGIGGKSFVTLTGDVASVESSVAAGVMLASER GMLVDKVVIPSPHDHLKRCLC