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PlpA plays a central role in lipid homeostasis in Gram-negative bacterial outer membranes
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
PlpA
Entity
1. PlpA (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
Exptl. method
solution NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 96.7 %, Completeness: 78.5 %, Completeness (bb): 90.1 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All78.5 % (1569 of 1999)71.7 % (731 of 1019)85.8 % (665 of 775)84.4 % (173 of 205)
Backbone90.1 % (979 of 1086)83.8 % (316 of 377)92.5 % (490 of 530)96.6 % (173 of 179)
Sidechain69.1 % (746 of 1079)64.6 % (415 of 642)80.5 % (331 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)
Methyl87.3 % (213 of 244)85.2 % (104 of 122)89.3 % (109 of 122)

1. PlpA

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


#NameIsotope labelingTypeConcentration
1PlpA[U-98% 13C; U-98% 15N]1.5 mM
2sodium phosphatenatural abundance50 mM
3sodium chloridenatural abundance50 mM
4sodium azidenatural abundance0.02 %
5H2Onatural abundance90 %
6D2Onatural abundance10 %

Release date
2014-02-18
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: 34552 released on 2020-09-07
    Title Structure-function analyses of dual-BON domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation to the cell division site
Related entities 1. PlpA, : 1 : 7 entities Detail
Experiments performed 13 experiments Detail
nullKeywords Gram negative, Outer membrane biogenesis, YraP, lipid biogenesis, lipoprotein