BMRB Entry 34738

Title:
Phosphatidylserine-dependent synaptic vesicle membrane sculpting by synaptogyrin
Deposition date:
2022-06-18
Original release date:
2023-05-19
Authors:
Yu, T.; Eastep, G.; Flores, D.; Zweckstetter, M.
Citation:

Citation: Yu, Taekyung; Flores-Solis, David; Eastep, Gunnar; Becker, Stefan; Zweckstetter, Markus. "Phosphatidylserine-dependent structure of synaptogyrin remodels the synaptic vesicle membrane"  Nat. Struct. Mol. Biol. 30, 926-934 (2023).
PubMed: 37217654

Assembly members:

Assembly members:
entity_1, polymer, 210 residues, 23356.428 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts561
15N chemical shifts182
1H chemical shifts1222

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 210 residues - 23356.428 Da.

1   METGLYHISHISHISHISHISHISHISALA
2   SERGLUASNLEUTYRPHEGLNGLYHISMET
3   GLUGLYGLYALATYRGLYALAGLYLYSALA
4   GLYGLYALAPHEASPPROTYRTHRLEUVAL
5   ARGGLNPROHISTHRILELEUARGVALVAL
6   SERTRPLEUPHESERILEVALVALPHEGLY
7   SERILEVALASNGLUGLYTYRLEUASNSER
8   ALASERGLUGLYGLUGLUPHECYSILETYR
9   ASNARGASNPROASNALACYSSERTYRGLY
10   VALALAVALGLYVALLEUALAPHELEUTHR
11   CYSLEULEUTYRLEUALALEUASPVALTYR
12   PHEPROGLNILESERSERVALLYSASPARG
13   LYSLYSALAVALLEUSERASPILEGLYVAL
14   SERALAPHETRPALAPHELEUTRPPHEVAL
15   GLYPHECYSTYRLEUALAASNGLNTRPGLN
16   VALSERLYSPROLYSASPASNPROLEUASN
17   GLUGLYTHRASPALAALAARGALAALAILE
18   ALAPHESERPHEPHESERILEPHETHRTRP
19   SERLEUTHRALAALALEUALAVALARGARG
20   PHELYSASPLEUSERPHEGLNGLUGLUTYR
21   SERTHRLEUPHEPROALASERALAGLNPRO

Samples:

sample_1: Synaptogyrin 1b, [U-15N], 0.8 mM

sample_2: Synaptogyrin 1b, [U-13C; U-15N; U-2H], 0.8 mM

sample_3: Synaptogyrin 1b, [U-15N; U-2H], 0.8 mM

sample_4: Synaptogyrin 1b, [U-100% 13C; U-100% 15N], 0.8 mM

sample_5: Synaptogyrin 1b, [U-15N], 0.8 mM

sample_conditions_1: ionic strength: 20 mM; pH: 8.5; pressure: 1 atm; temperature: 313 K

sample_conditions_2: ionic strength: 20 mM; pH: 8.5; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1anisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_4anisotropicsample_conditions_1
3D HNCOsample_2anisotropicsample_conditions_1
3D HN(CA)COsample_2anisotropicsample_conditions_1
3D HNCAsample_2anisotropicsample_conditions_1
3D HN(CO)CAsample_2anisotropicsample_conditions_1
3D HNCACBsample_3anisotropicsample_conditions_1
3D HNCBsample_3anisotropicsample_conditions_1
3D 1H-13C NOESYsample_4anisotropicsample_conditions_2
3D 1H-15N NOESYsample_3anisotropicsample_conditions_2
3D 1H-15N NOESYsample_5anisotropicsample_conditions_2

Software:

CcpNmr Analysis, CCPN - chemical shift assignment

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CYANA, Guntert, Mumenthaler and Wuthrich - peak picking

CS-ROSETTA, Shen, Vernon, Baker and Bax - structure calculation

NMR spectrometers:

  • Bruker AVANCE III HD 950 MHz
  • Bruker AVANCE III HD 900 MHz

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