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Found 1 Document (2.129 seconds)

BMRB: 5403

1C9S

Backbone resonance assignments of the 91 kDa oligomeric TRAP protein from Bacillus staerothermophilus in complex with L-tryptophan

Authors

McElroy, C.A., Manfredo, A., Wendt, A., Gollnick, P., Foster, M.P.

Assembly

trp RNA-binding attenuation protein undecamer

Entity

1. trp RNA-binding attenuation protein (polymer, Thiol state: not present), 74 monomers, 8242.252 × 11 Da Detail

MYTNSDFVVI KALEDGVNVI GLTRGADTRF HHSEKLDKGE VLIAQFTEHT SAIKVRGKAY IQTRHGVIES EGKK

2. TRYPTOPHAN (non-polymer), 1 monomers, 204.225 × 11 Da

Total weight

92911.25 Da

Max. entity weight

8242.252 Da

Source organism

Geobacillus stearothermophilus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 79.7 %, Completeness: 31.3 %, Completeness (bb): 59.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	31.3 % (267 of 854)	14.1 % (62 of 441)	44.5 % (149 of 335)	71.8 % (56 of 78)
Backbone	59.2 % (263 of 444)	37.4 % (58 of 155)	69.3 % (149 of 215)	75.7 % (56 of 74)
Sidechain	10.9 % (52 of 477)	1.4 % (4 of 286)	25.7 % (48 of 187)	0.0 % (0 of 4)
Aromatic	0.0 % (0 of 62)	0.0 % (0 of 31)	0.0 % (0 of 31)
Methyl	4.4 % (4 of 90)	0.0 % (0 of 45)	8.9 % (4 of 45)

1. trp RNA-binding attenuation protein

MYTNSDFVVI KALEDGVNVI GLTRGADTRF HHSEKLDKGE VLIAQFTEHT SAIKVRGKAY IQTRHGVIES EGKK

Show sample condition

Sample

Temperature 328 (±0.5) K, pH 8.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	trp RNA-binding attenuation protein	[U-2H; U-13C; U-15N]		6.6 mM
2	L-TRYPTOPHAN	[U-2H; U-13C; U-15N]		6.6 mM

Chem. Shift Complete2

Sequence coverage: 8.1 %, Completeness: 17.7 %, Completeness (bb): 32.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	17.7 % (302 of 1708)	9.1 % (80 of 882)	24.0 % (161 of 670)	39.1 % (61 of 156)
Backbone	32.7 % (290 of 888)	22.6 % (70 of 310)	37.0 % (159 of 430)	41.2 % (61 of 148)
Sidechain	6.5 % (62 of 954)	1.7 % (10 of 572)	13.9 % (52 of 374)	0.0 % (0 of 8)
Aromatic	0.0 % (0 of 124)	0.0 % (0 of 62)	0.0 % (0 of 62)
Methyl	4.4 % (8 of 180)	2.2 % (2 of 90)	6.7 % (6 of 90)

1. trp RNA-binding attenuation protein

MYTNSDFVVI KALEDGVNVI GLTRGADTRF HHSEKLDKGE VLIAQFTEHT SAIKVRGKAY IQTRHGVIES EGKK

Show sample condition

Sample

Temperature 328 (±0.5) K, pH 8.0 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	trp RNA-binding attenuation protein	[U-2H; U-13C; U-15N]		6.6 mM
2	L-TRYPTOPHAN	[U-2H; U-13C; U-15N]		6.6 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.66 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: 0.66 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	null	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291

Referencing offset: -1.12 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 1 models in PDB: 1C9S, Strand ID: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V Detail

Release date

2002-06-25

Citation 1

TROSY-NMR studies of the 91kDa TRAP protein reveal allosteric control of a gene regulatory protein by ligand-altered flexibility
McElroy, C.A., Manfredo, A., Wendt, A., Gollnick, P., Foster, M.P.
J. Mol. Biol. (2002), 323, 463-473, PubMed 12381302 , DOI 10.1016/s0022-2836(02)00940-3 , Abstract

Show more 11 citaions

Citation 2

11-fold symmetry of the trp RNA-binding attenuation protein (TRAP) from Bacillus subtilis determined by X-ray analysis
Antson, A.A., Brzozowski, A.M., Dodson, E.J., Dauter, Z., Wilson, K.S., Kurecki, T., Otridge, J., Gollnick, P.
J. Mol. Biol. (1994), 244, 1-5, PubMed 7525975 , DOI 10.1006/jmbi.1994.1698 , Abstract

Citation 3

Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA
Antson, A.A., Dodson, E.J., Dodson, G., Greaves, R.B., Chen, X., Gollnick, P.
Nature (1999), 401, 235-242, PubMed 10499579 , DOI 10.1038/45730 , Abstract

Citation 4

The structure of trp RNA-binding attenuation protein
Antson, A.A., Otridge, J., Brzozowski, A.M., Dodson, E.J., Dodson, G.G., Wilson, K.S., Smith, T.M., Yang, M., Kurecki, T., Gollnick, P.
Nature (1995), 374, 693-700, PubMed 7715723 , DOI 10.1038/374693a0 , Abstract

Citation 5

Regulation of tryptophan biosynthesis: Trp-ing the TRAP or how Bacillus subtilis reinvented the wheel
Babitzke, P.
Mol. Microbiol. (1997), 26, 1-9, PubMed 9383185 , Abstract

Citation 6

No title is available
null

Citation 7

Regulatory features of the trp operon and the crystal structure of the trp RNA-binding attenuation protein from Bacillus stearothermophilus
Chen, X., Antson, A.A., Yang, M., Li, P., Baumann, C., Dodson, E.J., Dodson, G.G., Gollnick, P.
J. Mol. Biol. (1999), 289, 1003-1016, PubMed 10369778 , DOI 10.1006/jmbi.1999.2834 , Abstract

Citation 8

The mtrB gene of Bacillus pumilus encodes a protein with sequence and functional homology to the trp RNA-binding attenuation protein (TRAP) of Bacillus subtilis
Hoffman, R.J., Gollnick, P.
J. Bacteriol. (1995), 177, 839-842, PubMed 7836324 , Abstract

Citation 9

cis-acting sites in the transcript of the Bacillus subtilis trp operon regulate expression of the operon
Kuroda, M.I., Henner, D., Yanofsky, C.
J. Bacteriol. (1988), 170, 3080-3088, PubMed 3133360 , Abstract

Citation 10

TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins
Salzmann, M., Pervushin, K., Wider, G., Senn, H., Wuthrich, K.
Proc. Natl. Acad. Sci. U. S. A. (1998), 95, 13585-13590, PubMed 9811843 , Abstract

Citation 11

Improved sensitivity and coherence selection for [15N,1H]-TROSY elements in triple resonance experiments
Salzmann, M., Wider, G., Pervushin, K., Wuthrich, K.
J. Biomol. NMR (1999), 15, 181-184, PubMed 10605091 , Abstract

Citation 12

Specificity of TRAP-RNA interactions: crystal structures of two complexes with different RNA sequences
Hopcroft, N.H., Wendt, A.L., Gollnick, P., Antson, A.A.
Acta Crystallogr. D. Biol. Crystallogr. (2002), 58, 615-621, PubMed 11914485 , DOI 10.1107/s0907444902003189 , Abstract

Hide non-primary 11 citaions

Entries sharing articles BMRB: 5, Swiss-Prot: 6 entries Detail

  BMRB: 15904 released on 2008-11-18
    Title 1J coupling constants related to the Ca carbons in oxidised Flavodoxin from Desulfovibrio vulgaris (Hildenborough)
  BMRB: 15905 released on 2008-11-18
    Title 1J coupling constants related to the Ca carbons in Ribonuclease T1 from Aspergillus oryzae
  BMRB: 15907 released on 2008-11-18
    Title 1J coupling constants related to the Ca carbons in human Ubiquitin
  BMRB: 15908 released on 2008-11-18
    Title 1J coupling constants related to the Ca carbons in Xylanase from Bacillus agaradhaerens
  BMRB: 15909 released on 2008-11-18
    Title 1J coupling constants related to the Ca carbons in DFPase from Loligo vulgaris
  Swiss-Prot: Q9X6J4 released on 2000-05-30
    Title TRPE_GEOSE Entity Anthranilate synthase component 1
  Swiss-Prot: Q9X6J5 released on 2000-05-30
    Title TRPD_GEOSE Entity Anthranilate phosphoribosyltransferase
  Swiss-Prot: Q9X6J6 released on 2000-05-30
    Title MTRB_GEOSE Entity Transcription attenuation protein MtrB
  Swiss-Prot: P48063 released on 1996-02-01
    Title GCH1_BACPU Entity GTP cyclohydrolase 1
  Swiss-Prot: P48064 released on 1996-02-01
    Title MTRB_BACPU Entity Transcription attenuation protein MtrB
  Swiss-Prot: P19466 released on 1991-02-01
    Title MTRB_BACSU Entity Transcription attenuation protein MtrB

Related entities 1. trp RNA-binding attenuation protein, : 1 : 21 : 7 : 11 entities Detail

Interaction partners 1. trp RNA-binding attenuation protein, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 5 experiments Detail

nullKeywords Bacillus stearothermophilus, NMR assignments, TROSY, trp RNA-binding attenuation protein

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Found 1 Document (2.129 seconds)

BMRB: 5403

Sample

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Entries sharing articles BMRB: 5, Swiss-Prot: 6 entries Detail

Related entities 1. trp RNA-binding attenuation protein, : 1 : 21 : 7 : 11 entities Detail

Interaction partners 1. trp RNA-binding attenuation protein, : 1 interactors Detail

Experiments performed 5 experiments Detail

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