BMRB Entry 31232

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31232

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Title:
Dimeric Structure of full-length CrgA, a Cell Division Protein from Mycobacterium tuberculosis, in Lipid Bilayers
Deposition date:
2025-03-03
Original release date:
2025-04-07
Authors:
Shin, Y.; Prasad, R.; Das, N.; Taylor, J.; Qin, H.; Hu, W.; Hu, Y.-Y., Y.; Fu, R.; Zhang, R.; Zhou, H.-X., H.; Cross, T.
Citation:

Citation: Shin, Y.; Prasad, R.; Das, N.; Taylor, J.; Qin, H.; Hu, W.; Hu, Y.; Fu, R.; Zhang, R.; Zhou, H.; Cross, T.. "Mycobacterium tuberculosis CrgA Forms a Dimeric Structure with Its Transmembrane Domain Sandwiched between Cytoplasmic and Periplasmic beta-Sheets, Enabling Multiple Interactions with Other Divisome Proteins."  J.Am.Chem.Soc. ., .-. (2025).
PubMed: 40106808

Assembly members:

Assembly members:
entity_1, polymer, 102 residues, 11641.963 Da.

Natural source:

Natural source:   Common Name: Mycobacterium tuberculosis H37Rv   Taxonomy ID: 83332   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MMPKSKVRKKNDFTVSAVSR TPMKVKVGPSSVWFVSLFIG LMLIGLIWLMVFQLAAIGSQ APTALNWMAQLGPWNYAIAF AFMITGLLLTMRWHLEHHHH HH

Data sets:
Data typeCount
15N chemical shifts69

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_21

Entities:

Entity 1, unit_1 102 residues - 11641.963 Da.

1   METMETPROLYSSERLYSVALARGLYSLYS
2   ASNASPPHETHRVALSERALAVALSERARG
3   THRPROMETLYSVALLYSVALGLYPROSER
4   SERVALTRPPHEVALSERLEUPHEILEGLY
5   LEUMETLEUILEGLYLEUILETRPLEUMET
6   VALPHEGLNLEUALAALAILEGLYSERGLN
7   ALAPROTHRALALEUASNTRPMETALAGLN
8   LEUGLYPROTRPASNTYRALAILEALAPHE
9   ALAPHEMETILETHRGLYLEULEULEUTHR
10   METARGTRPHISLEUGLUHISHISHISHIS
11   HISHIS

Samples:

sample_1: CrgA-Ala, [U-15N]-Ala, 200 mg/L; CrgA-Val, [U-15N]-Val, 200 mg/L; CrgA-Leu,Thr, [U-15N]-Leu, [U-15N]-Thr, 200 mg/L; CrgA-Met, [U-15N]-Met, 200 mg/L; CrgA-Phe, [U-15N]-Phe, 200 mg/L; CrgA-Trp, [U-15N]-Trp, 200 mg/L; CrgA-Gly, [U-15N]-Gly, 200 mg/L; CrgA-Ile, [U-15N]-Ile, 200 mg/L; CrgA-Tyr, [U-15N]-Tyr, 200 mg/L

sample_2: CrgA-Arg, [U-15N]-NH4Cl, 1 g/L; CrgA-Asn,Lys,Ser, [U-15N]-NH4Cl, 1 g/L

sample_3: CrgA-Val, [U-13C]-Val, 200 mg/L; CrgA-Met, [U-13C]-Met, 200 mg/L; CrgA-Phe, [U-13C]-Phe, 200 mg/L; CrgA-Met,Ala, [U-13C]-Met,[U-13C]-Ala, 200 mg/L; CrgA-Leu,Tyr, [U-13C]-Leu,[U-13C]-Tyr, 200 mg/L; CrgA-Lys, [U-13C]-Lys, 200 mg/L

sample_conditions_1: ionic strength: 5 mM; pH: 8.0; pressure: 1 atm; temperature: 289 K

sample_conditions_2: ionic strength: 5 mM; pH: 8.0; pressure: 1 atm; temperature: 265 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N PISEMAsample_1anisotropicsample_conditions_1
2D 1H-15N PISEMAsample_2anisotropicsample_conditions_1
2D 13C-13C DARRsample_3isotropicsample_conditions_2

Software:

NAMD v2.13, Phillips, Braun, Wang, Gumbart, Tajkhorshid, Villa, Chipot, Skeel, Kale and Schulten - refinement

X-PLOR NIH v3.4, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

TopSpin, Bruker Biospin - chemical shift assignment, data analysis, peak picking, processing

NMR spectrometers:

  • Bruker AVANCE 600 MHz
  • Bruker AVANCE 600 MHz