11-FOLD SYMMETRY OF THE TRP RNA-BINDING ATTENUATION PROTEIN (TRAP) FROM BACILLUS-SUBTILIS DETERMINED BY X-RAY-ANALYSIS

A A  ANTSON; A M  BRZOZOWSKI; E J  DODSON; Z  DAUTER; K S  WILSON; T  KURECKI; J  OTRIDGE; P  GOLLNICK

11-FOLD SYMMETRY OF THE TRP RNA-BINDING ATTENUATION PROTEIN (TRAP) FROM BACILLUS-SUBTILIS DETERMINED BY X-RAY-ANALYSIS

A A ANTSON, A M BRZOZOWSKI, E J DODSON, Z DAUTER, K S WILSON, T KURECKI, J OTRIDGE, P GOLLNICK

Chemistry

Research output: Contribution to journal › Comment/debate › peer-review

Abstract

The trp RNA-binding attenuation protein (TRAP) of Bacillus subtilis has been crystallized and examined by crystallography using X-ray synchrotron radiation diffraction data. Crystals of TRAP complexed with L-tryptophan belong to space group C2 with a = 156.8 Angstrom, b = 114.05 Angstrom, c = 105.9 Angstrom, beta = 118.2 degrees. Crystals of a potential heavy-atom derivative of TRAP complexed with 5-bromo-L-tryptophan grow in the same space group with similar cell dimensions. X-ray data for the native crystals and for the derivative have been collected to 2.9 Angstrom and 2.2 Angstrom resolution, respectively. Peaks in the self-rotation function and in the Patterson synthesis could only be explained by two 11-subunit oligomers (each formed by an 11-fold axis of symmetry) in the asymmetric unit lying with the 11-fold rotation axes parallel to each other. The consequence is that the TRAP molecule has 11-fold symmetry and contains 11 subunits.

Original language	English
Pages (from-to)	15
Number of pages	5
Journal	Journal of Molecular Biology
Volume	244
Issue number	1
Publication status	Published - 18 Nov 1994

Keywords

TRP ATTENUATION PROTEIN
RNA-BINDING PROTEIN
CRYSTALLIZATION
X-RAY ANALYSIS
TRANSCRIPTION ATTENUATION
OPERON
EXPRESSION
MTRB

Cite this

@article{f066af53bc7f452380e85352354289d9,

title = "11-FOLD SYMMETRY OF THE TRP RNA-BINDING ATTENUATION PROTEIN (TRAP) FROM BACILLUS-SUBTILIS DETERMINED BY X-RAY-ANALYSIS",

abstract = "The trp RNA-binding attenuation protein (TRAP) of Bacillus subtilis has been crystallized and examined by crystallography using X-ray synchrotron radiation diffraction data. Crystals of TRAP complexed with L-tryptophan belong to space group C2 with a = 156.8 Angstrom, b = 114.05 Angstrom, c = 105.9 Angstrom, beta = 118.2 degrees. Crystals of a potential heavy-atom derivative of TRAP complexed with 5-bromo-L-tryptophan grow in the same space group with similar cell dimensions. X-ray data for the native crystals and for the derivative have been collected to 2.9 Angstrom and 2.2 Angstrom resolution, respectively. Peaks in the self-rotation function and in the Patterson synthesis could only be explained by two 11-subunit oligomers (each formed by an 11-fold axis of symmetry) in the asymmetric unit lying with the 11-fold rotation axes parallel to each other. The consequence is that the TRAP molecule has 11-fold symmetry and contains 11 subunits.",

keywords = "TRP ATTENUATION PROTEIN, RNA-BINDING PROTEIN, CRYSTALLIZATION, X-RAY ANALYSIS, TRANSCRIPTION ATTENUATION, OPERON, EXPRESSION, MTRB",

author = "ANTSON, {A A} and BRZOZOWSKI, {A M} and DODSON, {E J} and Z DAUTER and WILSON, {K S} and T KURECKI and J OTRIDGE and P GOLLNICK",

year = "1994",

month = nov,

day = "18",

language = "English",

volume = "244",

pages = "15",

journal = "Journal of Molecular Biology",

issn = "0022-2836",

publisher = "Academic Press",

number = "1",

}

TY - JOUR

T1 - 11-FOLD SYMMETRY OF THE TRP RNA-BINDING ATTENUATION PROTEIN (TRAP) FROM BACILLUS-SUBTILIS DETERMINED BY X-RAY-ANALYSIS

AU - ANTSON, A A

AU - BRZOZOWSKI, A M

AU - DODSON, E J

AU - DAUTER, Z

AU - WILSON, K S

AU - KURECKI, T

AU - OTRIDGE, J

AU - GOLLNICK, P

PY - 1994/11/18

Y1 - 1994/11/18

N2 - The trp RNA-binding attenuation protein (TRAP) of Bacillus subtilis has been crystallized and examined by crystallography using X-ray synchrotron radiation diffraction data. Crystals of TRAP complexed with L-tryptophan belong to space group C2 with a = 156.8 Angstrom, b = 114.05 Angstrom, c = 105.9 Angstrom, beta = 118.2 degrees. Crystals of a potential heavy-atom derivative of TRAP complexed with 5-bromo-L-tryptophan grow in the same space group with similar cell dimensions. X-ray data for the native crystals and for the derivative have been collected to 2.9 Angstrom and 2.2 Angstrom resolution, respectively. Peaks in the self-rotation function and in the Patterson synthesis could only be explained by two 11-subunit oligomers (each formed by an 11-fold axis of symmetry) in the asymmetric unit lying with the 11-fold rotation axes parallel to each other. The consequence is that the TRAP molecule has 11-fold symmetry and contains 11 subunits.

AB - The trp RNA-binding attenuation protein (TRAP) of Bacillus subtilis has been crystallized and examined by crystallography using X-ray synchrotron radiation diffraction data. Crystals of TRAP complexed with L-tryptophan belong to space group C2 with a = 156.8 Angstrom, b = 114.05 Angstrom, c = 105.9 Angstrom, beta = 118.2 degrees. Crystals of a potential heavy-atom derivative of TRAP complexed with 5-bromo-L-tryptophan grow in the same space group with similar cell dimensions. X-ray data for the native crystals and for the derivative have been collected to 2.9 Angstrom and 2.2 Angstrom resolution, respectively. Peaks in the self-rotation function and in the Patterson synthesis could only be explained by two 11-subunit oligomers (each formed by an 11-fold axis of symmetry) in the asymmetric unit lying with the 11-fold rotation axes parallel to each other. The consequence is that the TRAP molecule has 11-fold symmetry and contains 11 subunits.

KW - TRP ATTENUATION PROTEIN

KW - RNA-BINDING PROTEIN

KW - CRYSTALLIZATION

KW - X-RAY ANALYSIS

KW - TRANSCRIPTION ATTENUATION

KW - OPERON

KW - EXPRESSION

KW - MTRB

M3 - Comment/debate

SN - 0022-2836

VL - 244

SP - 15

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 1

ER -