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Structure-function analyses of dual-BON domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation to the cell division site
Authors
Morris, F.C., Knowles, T.J., Maderbocus, R., Jeeves, M., Kirwan, J., Heinz, E., Wells, T.J., Browning, D.F., Sevastsyanovich, Y.R., Leyton, D.L., Rossiter, A.E., Bavro, V.N., Sridhar, P., Ward, D.G., Shimwell, N.J., Martin, A., Sahl, J.W., Wardius, C.A., Walker, D., Lithgow, T., Viant, M.R., Rasko, D.A., Cunningham, A.F., Overduin, M., Henderson, I.R.
Assembly
DolP
Entity
1. DolP (polymer, Thiol state: not present), 182 monomers, 19297.50 Da Detail

IAAAVVGTAA VGTKAATDPR SVGTQVDDGT LEVRVNSALS KDEQIKKEAR INVTAYQGKV LLVGQSPNAE LSARAKQIAM GVDGANEVYN EIRQGQPIGL GEASNDTWIT TKVRSQLLTS DLVKSSNVKV TTENGEVFLM GLVTEREAKA AADIASRVSG VKRVTTAFTF IKGGLEHHHH HH


Formula weight
19297.5 Da
Source organism
Escherichia coli KTE10
Exptl. method
solution NMR
Data set
assigned_chemical_shifts, spectral_peak_list
Chem. Shift Complete
Sequence coverage: 96.7 %, Completeness: 83.6 %, Completeness (bb): 94.3 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All83.6 % (1671 of 1999)79.3 % (808 of 1019)89.2 % (691 of 775)83.9 % (172 of 205)
Backbone94.3 % (1024 of 1086)91.2 % (344 of 377)95.8 % (508 of 530)96.1 % (172 of 179)
Sidechain74.7 % (806 of 1079)72.1 % (463 of 642)83.5 % (343 of 411) 0.0 % (0 of 26)
Aromatic42.7 % (35 of 82)43.9 % (18 of 41)42.5 % (17 of 40) 0.0 % (0 of 1)
Methyl91.8 % (224 of 244)91.8 % (112 of 122)91.8 % (112 of 122)

1. entity 1

IAAAVVGTAA VGTKAATDPR SVGTQVDDGT LEVRVNSALS KDEQIKKEAR INVTAYQGKV LLVGQSPNAE LSARAKQIAM GVDGANEVYN EIRQGQPIGL GEASNDTWIT TKVRSQLLTS DLVKSSNVKV TTENGEVFLM GLVTEREAKA AADIASRVSG VKRVTTAFTF IKGGLEHHHH HH

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6 (±0.05), Details 1.5 mM [U-13C; U-15N] DolP, 50 mM NA sodium phosphate, 0.02 % w/v NA NaN3, 50 mM NA sodium chloride, 90% H2O/10% D2O


#NameIsotope labelingTypeConcentration
1DolP[U-13C; U-15N]1.5 mM
2sodium phosphatenatural abundance50 mM
3NaN3natural abundance0.02 % w/v
4sodium chloridenatural abundance50 mM

Release date
2020-09-07
Citation
Structure of dual BON-domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation
Bryant, J.A., Morris, F.C., Knowles, T.J., Maderbocus, R., Heinz, E., Boelter, G., Alodaini, D., Colyer, A., Wotherspoon, P.J., Staunton, K.A., Jeeves, M., Browning, D.F., Sevastsyanovich, Y.R., Wells, T.J., Rossiter, A.E., Bavro, V.N., Sridhar, P., Ward, D.G., Chong, Z.S., Goodall, E.C., Icke, C., Teo, A.C., Chng, S.S., Roper, D.I., Lithgow, T., Cunningham, A.F., Banzhaf, M., Overduin, M., Henderson, I.R.
Elife (2020), 9, PubMed 33315009 , DOI 10.7554/eLife.62614 ,
Entries sharing articles BMRB: 1 entries Detail
  BMRB: 19760 released on 2014-02-18
    Title PlpA plays a central role in lipid homeostasis in Gram-negative bacterial outer membranes
Related entities 1. DolP, : 1 : 7 entities Detail
Experiments performed 13 experiments Detail
Chemical shift validation 3 contents Detail
Keywords GRAM NEGATIVE, LIPID BIOGENESIS, LIPOPROTEIN, OUTER MEMBRANE BIOGENESIS, PROTEIN BINDING, YRAP