BMRB Entry 17006

Title:
Solution structure of alpha-mannosidase binding domain of Atg19
Deposition date:
2010-06-18
Original release date:
2010-08-12
Authors:
Watanabe, Yasunori; Noda, Nobuo N; Kumeta, Hiroyuki; Suzuki, Kuninori; Ohsumi, Yoshinori; Inagaki, Fuyuhiko
Citation:

Citation: Watanabe, Yasunori; Noda, Nobuo; Kumeta, Hiroyuki; Suzuki, Kuninori; Ohsumi, Yoshinori; Inagaki, Fuyuhiko. "Selective Transport of {alpha}-Mannosidase by Autophagic Pathways: STRUCTURAL BASIS FOR CARGO RECOGNITION BY Atg19 AND Atg34."  J. Biol. Chem. 285, 30026-30033 (2010).
PubMed: 20659891

Assembly members:

Assembly members:
Atg19, polymer, 118 residues, 12965.639 Da.

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-6p-1

Data sets:
Data typeCount
13C chemical shifts491
15N chemical shifts118
1H chemical shifts808

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Atg191

Entities:

Entity 1, Atg19 118 residues - 12965.639 Da.

1   GLYPROHISMETVALGLUPROPROASNGLU
2   ARGSERLEUGLNILETHRMETASNGLNARG
3   ASPASNSERLEUTYRPHEGLNLEUPHEASN
4   ASNTHRASNSERVALLEUALAGLYASNCYS
5   LYSLEULYSPHETHRASPALAGLYASPLYS
6   PROTHRTHRGLNILEILEASPMETGLYPRO
7   HISGLUILEGLYILELYSGLUTYRLYSGLU
8   TYRARGTYRPHEPROTYRALALEUASPLEU
9   GLUALAGLYSERTHRILEGLUILEGLUASN
10   GLNTYRGLYGLUVALILEPHELEUGLYLYS
11   TYRGLYSERSERPROMETILEASNLEUARG
12   PROPROSERARGLEUSERALAGLU

Samples:

sample_1: sodium phosphate 25 mM; sodium chloride 100 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)HAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D (Hb)Cb(CgCd)Hdsample_1isotropicsample_conditions_1
2D (Hb)Cb(CgCdCe)Hesample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

SPARKY, Goddard - chemical shift assignment, peak picking

VNMR, Varian - collection

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

PDB
DBJ GAA26246
EMBL CAA53201 CAA58199 CAA99094 CAY86211
GB AAT93193 AHY77232 AJP41464 AJT70883 AJT71374
REF NP_014559
SP A6ZNC8 P35193
TPG DAA10702
AlphaFold A6ZNC8 P35193

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