BMRB Entry 51880

Title:
Assignments for plectasin in complex with Lipid II in membranes
Deposition date:
2023-03-20
Original release date:
2024-05-02
Authors:
Derks, Maik
Citation:

Citation: Jekhmane, Shehrazade; Derks, Maik; Maity, Sourav; Slingerland, Cornelis; Tehrani, Kamaleddin; Medeiros-Silva, Joao; Charitou, Vicky; Ammerlaan, Danique; Fetz, Celine; Consoli, Naomi; Cochrane, Rachel; Matheson, Eilidh; van der Weijde, Mick; Elenbaas, Barend; Lavore, Francesca; Cox, Ruud; Lorent, Joseph; Baldus, Marc; Kunzler, Markus; Lelli, Moreno; Cochrane, Stephen; Martin, Nathaniel; Roos, Wouter; Breukink, Eefjan; Weingarth, Markus. "Host defence peptide plectasin targets bacterial cell wall precursor lipid II by a calcium-sensitive supramolecular mechanism"  Nat. Microbiol. 9, 1778-1791 (2024).
PubMed: 38783023

Assembly members:

Assembly members:
entity_1, polymer, 40 residues, Formula weight is not available
entity_2, polymer, 7 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-SUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GFGCNGPWDEDDMQCHNHCK SIKGYKGGYCAKGGFVCKCY
entity_2: AXKXXXX

Data typeCount
13C chemical shifts197
15N chemical shifts202
1H chemical shifts202

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Plectasin1
2Lipid II2

Entities:

Entity 1, Plectasin 40 residues - Formula weight is not available

1   GLYPHEGLYCYSASNGLYPROTRPASPGLU
2   ASPASPMETGLNCYSHISASNHISCYSLYS
3   SERILELYSGLYTYRLYSGLYGLYTYRCYS
4   ALALYSGLYGLYPHEVALCYSLYSCYSTYR

Entity 2, Lipid II 7 residues - Formula weight is not available

1   ALAFGALYSDALDALMUBNAG

Samples:

sample_1: plectasin, [U-100% 13C; U-100% 15N], 400 nmol; Lipid II 400 nmol; H2O 100%; beta-mercaptoethanol 1 mM; sodium phosphate 50 mM; sodium chloride 150 mM; DOPC 9.6 umol

sample_2: plectasin, [U-100% 15N], 400 nmol; Lipid II lysine form C55, [U-100% 13C; U-100% 15N], 400 nmol; H2O 100%; beta-mercaptoethanol 1 mM; sodium phosphate 50 mM; sodium chloride 150 mM; DOPC 9.6 umol

sample_3: plectasin, [U-100% 13C; U-100% 15N], 100 nmol; Lipid II lysine form C55 100 nmol; H2O 100%; beta-mercaptoethanol 1 mM; HEPES 50 mM; sodium chloride 150 mM; DOPC 2.4 umol; Calcium 1 mM

sample_4: plectasin, [U-100% 13C; U-100% 15N], 100 nmol; Lipid II lysine form C55 100 nmol; H2O 100%; beta-mercaptoethanol 1 mM; HEPES 50 mM; sodium chloride 150 mM; DOPG 2.4 umol; Calcium 1 mM

sample_5: plectasin, [U-100% 13C; U-100% 15N], 100 nmol; Lipid II lysine form C55 100 nmol; H2O 100%; beta-mercaptoethanol 1 mM; HEPES 50 mM; sodium chloride 150 mM; DOPG 2.4 umol; Magnesium 1 mM

sample_6: plectasin, [U-100% 13C; U-100% 15N], 100 nmol; Lipid II lysine form C55 100 nmol; H2O 100%; beta-mercaptoethanol 1 mM; sodium phosphate 50 mM; sodium chloride 150 mM; DOPG 2.4 umol

sample_conditions_1: pH: 7.2; pressure: 1 atm; temperature: 270 K

sample_conditions_2: pH: 7.2; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D PARIS CCsample_1isotropicsample_conditions_1
2D (H)NHsample_1isotropicsample_conditions_2
2D (H)NHsample_3isotropicsample_conditions_2
2D (H)NHsample_4isotropicsample_conditions_2
2D (H)NHsample_5isotropicsample_conditions_2
2D (H)NHsample_6isotropicsample_conditions_2
2D PARIS CCsample_2isotropicsample_conditions_1
2D 13C/13C TOBSYsample_2isotropicsample_conditions_2

Software:

TOPSPIN - collection, processing

POKY - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE III 950 MHz
  • Bruker AVANCE NEO 1200 MHz
  • Bruker Avance 700 MHz