BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19760

Title: PlpA plays a central role in lipid homeostasis in Gram-negative bacterial outer membranes   PubMed: 33315009

Deposition date: 2014-02-03 Original release date: 2022-06-10

Authors: Morris, Faye; Knowles, Timothy; Maderbocus, Riyaz; Jeeves, Mark; Kirwan, Jennifer; Heinz, Eva; Wells, Timothy; Browning, Douglas; Sevastsyanovich, Yanina; Leyton, Denisse; Rossiter, Amanda; Bavro, Vassiliy; Sridhar, Pooja; Ward, Douglas; Shimwell, Neil; Martin, Ashley; Sahl, Jason; Wardius, Catherine; Walker, Daniel; Lithgow, Trevor; Viant, Mark; Rasko, David; Cunningham, Adam; Overduin, Michael; Henderson, Ian

Citation: Bryant, Jack Alfred; Morris, Faye; Knowles, Timothy; Maderbocus, Riyaz; Heinz, Eva; Boelter, Gabriela; Alodaini, Dema; Colyer, Adam; Wotherspoon, Peter; Staunton, Kara; Jeeves, Mark; Browning, Douglas; Sevastsyanovich, Yanina; Wells, Timothy; Rossiter, Amanda; Bavro, Vassiliy; Sridhar, Pooja; Ward, Douglas; Chong, Zhi-Soon; Goodall, Emily Ca; Icke, Christopher; Teo, Alvin Ck; Chng, Shu-Sin; Roper, David; Lithgow, Trevor; Cunningham, Adam; Banzhaf, Manuel; Overduin, Michael; Henderson, Ian. "Structure of dual BON-domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation"  Elife 9, .-. (2020).

Assembly members:
PlpA, polymer, 182 residues, 18772.311 Da.

Natural source:   Common Name: enterobacteria   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET26b

Entity Sequences (FASTA):
PlpA: IAAAVVGTAAVGTKAATDPR SVGTQVDDGTLEVRVNSALS KDEQIKKEARINVTAYQGKV LLVGQSPNAELSARAKQIAM GVDGANEVYNEIRQGQPIGL GEASNDTWITTKVRSQLLTS DLVKSSNVKVTTENGEVFLM GLVTEREAKAAADIASRVSG VKRVTTAFTFIKGGLEHHHH HH

Data sets:
Data typeCount
13C chemical shifts686
15N chemical shifts172
1H chemical shifts1023

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 182 residues - 18772.311 Da.

Residue 20 - represents non-native sequence. Replacement of Val with Ile due to cloning Residues 192-195 - Non-native due to cloning strategy Residues 196-201 - Non native - His Tag

1   ILEALAALAALAVALVALGLYTHRALAALA
2   VALGLYTHRLYSALAALATHRASPPROARG
3   SERVALGLYTHRGLNVALASPASPGLYTHR
4   LEUGLUVALARGVALASNSERALALEUSER
5   LYSASPGLUGLNILELYSLYSGLUALAARG
6   ILEASNVALTHRALATYRGLNGLYLYSVAL
7   LEULEUVALGLYGLNSERPROASNALAGLU
8   LEUSERALAARGALALYSGLNILEALAMET
9   GLYVALASPGLYALAASNGLUVALTYRASN
10   GLUILEARGGLNGLYGLNPROILEGLYLEU
11   GLYGLUALASERASNASPTHRTRPILETHR
12   THRLYSVALARGSERGLNLEULEUTHRSER
13   ASPLEUVALLYSSERSERASNVALLYSVAL
14   THRTHRGLUASNGLYGLUVALPHELEUMET
15   GLYLEUVALTHRGLUARGGLUALALYSALA
16   ALAALAASPILEALASERARGVALSERGLY
17   VALLYSARGVALTHRTHRALAPHETHRPHE
18   ILELYSGLYGLYLEUGLUHISHISHISHIS
19   HISHIS

Samples:

sample_1: PlpA, [U-98% 13C; U-98% 15N], 1.5 mM; sodium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D H(C)CH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY-HSQC aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY-HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESY-HSQCsample_1isotropicsample_conditions_1
H(C)CONHsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

ARIA v2.3, Linge, O'Donoghue and Nilges - refinement

SPARKY, Goddard - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

ProcheckNMR, Laskowski and MacArthur - refinement

NMR spectrometers:

  • Varian INOVA 800 MHz

Related Database Links:

UNP P64596
AlphaFold Q2M960

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts